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Conserved domains on  [gi|27229145|ref|NP_082307|]
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palmitoyltransferase ZDHHC13 [Mus musculus]

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];
30-289 2.26e-38

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 143.56  E-value: 2.26e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145  30 HENKELAKAKEILPLIEDSSNCDIVKATQYGIFERCKELVEAGYDVRQPDRENVSLLHWAAINNRLELVKFYISKGAVID 109
Cdd:COG0666  35 LLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVN 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145 110 QLGGDlNSTPLHWAIRQGHLPMVILLLQHGADPTLIDGEGFSSIHLAVLFQHMPIIAYLISKGQSVNMTDVNGqtplmls 189
Cdd:COG0666 115 ARDKD-GETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDG------- 186

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145 190 aykvigpeptgfllkfnpslsvvdkthqNTPLHWAVAAGNVSAVDKLLEAGSSLDIRNAKGETPLDMALQSKNQLISHML 269
Cdd:COG0666 187 ----------------------------ETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLL 238

                       250       260
                ....*....|....*....|
gi 27229145 270 RTEAKMRANKQFRLWRWLHK 289
Cdd:COG0666 239 LEAGADLNAKDKDGLTALLL 258
DHHC pfam01529
DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which ...
 423-557 5.03e-33

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: 123.25  E-value: 5.03e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145   423 DFRTFCTSCLIRKPLRSLHCHVCNSCVARFDQHCFWTGRCIGFGNHHHYIFFLLSLSMVCDWIIYGSFVYWSNHCATTFK 502
Cdd:pfam01529   3 DELKYCSTCNIYKPPRSKHCRVCNRCVLRFDHHCPWLNNCIGKRNHKYFILFLLYLTLYLILYLVLSLYYLVKLIESSTL 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 27229145   503 EDGLWTYLNQivacspWVLYIFMLAAFHFSWSTFLLINQLFQIaFLGLTSHERIS 557
Cdd:pfam01529  83 FFFLILFLFS------ISIILLILSLFFLLFLGILLFFHLYLI-SRNLTTYEFMK 130
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
30-289 2.26e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 143.56  E-value: 2.26e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145  30 HENKELAKAKEILPLIEDSSNCDIVKATQYGIFERCKELVEAGYDVRQPDRENVSLLHWAAINNRLELVKFYISKGAVID 109
Cdd:COG0666  35 LLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVN 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145 110 QLGGDlNSTPLHWAIRQGHLPMVILLLQHGADPTLIDGEGFSSIHLAVLFQHMPIIAYLISKGQSVNMTDVNGqtplmls 189
Cdd:COG0666 115 ARDKD-GETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDG------- 186

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145 190 aykvigpeptgfllkfnpslsvvdkthqNTPLHWAVAAGNVSAVDKLLEAGSSLDIRNAKGETPLDMALQSKNQLISHML 269
Cdd:COG0666 187 ----------------------------ETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLL 238

                       250       260
                ....*....|....*....|
gi 27229145 270 RTEAKMRANKQFRLWRWLHK 289
Cdd:COG0666 239 LEAGADLNAKDKDGLTALLL 258
DHHC pfam01529
DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which ...
 423-557 5.03e-33

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: 123.25  E-value: 5.03e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145   423 DFRTFCTSCLIRKPLRSLHCHVCNSCVARFDQHCFWTGRCIGFGNHHHYIFFLLSLSMVCDWIIYGSFVYWSNHCATTFK 502
Cdd:pfam01529   3 DELKYCSTCNIYKPPRSKHCRVCNRCVLRFDHHCPWLNNCIGKRNHKYFILFLLYLTLYLILYLVLSLYYLVKLIESSTL 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 27229145   503 EDGLWTYLNQivacspWVLYIFMLAAFHFSWSTFLLINQLFQIaFLGLTSHERIS 557
Cdd:pfam01529  83 FFFLILFLFS------ISIILLILSLFFLLFLGILLFFHLYLI-SRNLTTYEFMK 130
COG5273 COG5273
Uncharacterized protein containing DHHC-type Zn finger [General function prediction only];
341-588 1.16e-27

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


Pssm-ID: 227598 [Multi-domain]  Cd Length: 309  Bit Score: 113.69  E-value: 1.16e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145 341 YKNLVYLPTVFLLSSIFWIFMTwFILFFPDTAGSPLYFAFIFSIMAFLYFFYKTwaTDPGF--TKASEEERKVNIVTLAE 418
Cdd:COG5273  26 YAYKMFIGLFLLSRIVVYTLLV-IVKSLSLVVLFIILFIVILVLASFSYLLLLV--SDPGYlgENITLSGYRETISRLLD 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145 419 TGSLDFRTFCTSCLIRKPLRSLHCHVCNSCVARFDQHCFWTGRCIGFGNHHHYIFFLLslsmvcdWIIYGSFVYWSNHCA 498
Cdd:COG5273 103 DGKFGTENFCSTCNIYKPPRSHHCSICNRCVLKFDHHCPWINNCVGFRNYRFFYQFLL-------YTILVALVVLLSTAY 175

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145 499 TTFKEDGLWTYLNQIV-------ACSPWVLYIFMLAAFHFswSTFLLINQLFQIAFL----GLTSHERISLLKQS-RHMK 566
Cdd:COG5273 176 YIAGIFSIRHDTSLAIcflifgcSLLGVVFFIITTLLLLF--LIYLILNNLTTIEFIqisrGGSTLEFFPLCRESnLPFT 253

                       250       260
                ....*....|....*....|....
gi 27229145 567 QTLSLRKT--PYNLGFTQNLADFF 588
Cdd:COG5273 254 NIFDSSEGalPLDLGIGQNLSTIK 277
Ank_2 pfam12796
Ankyrin repeats (3 copies);
56-146 3.33e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.77  E-value: 3.33e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145    56 ATQYGIFERCKELVEAGYDVRQPDRENVSLLHWAAINNRLELVKFYISKGAVIDQLGGDlnsTPLHWAIRQGHLPMVILL 135
Cdd:pfam12796   4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR---TALHYAARSGHLEIVKLL 80

                          90
                  ....*....|.
gi 27229145   136 LQHGADPTLID 146
Cdd:pfam12796  81 LEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 66-269 5.71e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 83.56  E-value: 5.71e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145   66 KELVEAGYDVRQPDRENVSLLHWAA-----INNRLELVKFYISKGAVIDQlGGDLNSTPLHWAI--RQGHLPMVILLLQH 138
Cdd:PHA03100  52 KILLDNGADINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLEYGANVNA-PDNNGITPLLYAIskKSNSYSIVEYLLDN 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145  139 GADPTLIDGEGFSSIHLAVLFQH--MPIIAYLISKGQSVN-MTDVNgqtplmlsaykvigpeptgFLLKFNPSLSVVDKt 215
Cdd:PHA03100 131 GANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINaKNRVN-------------------YLLSYGVPINIKDV- 190

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 27229145  216 HQNTPLHWAVAAGNVSAVDKLLEAGSSLDIRNAKGETPLDMALQSKNQLISHML 269
Cdd:PHA03100 191 YGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLL 244
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 118-144 2.63e-05

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: 41.42  E-value: 2.63e-05
                           10        20
                   ....*....|....*....|....*..
gi 27229145    118 TPLHWAIRQGHLPMVILLLQHGADPTL 144
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 77-268 1.33e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 45.00  E-value: 1.33e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145  77 QPDRENVSLLHWAAINNRLELVKfYISKGAVIDQLG-GDLNSTPLHWAIRQGHLPMVILLLQhgADPTLIDG-------E 148
Cdd:cd22192  12 QQKRISESPLLLAAKENDVQAIK-KLLKCPSCDLFQrGALGETALHVAALYDNLEAAVVLME--AAPELVNEpmtsdlyQ 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145 149 GFSSIHLAVLFQHMPIIAYLISKGQSVnmtdvngqtplmlsaykvIGPEPTGFLLKFNPSLSVVDKTHqntPLHWAVAAG 228
Cdd:cd22192  89 GETALHIAVVNQNLNLVRELIARGADV------------------VSPRATGTFFRPGPKNLIYYGEH---PLSFAACVG 147

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 27229145 229 NVSAVDKLLEAGSSLDIRNAKGETPLDM-ALQSKNQLISHM 268
Cdd:cd22192 148 NEEIVRLLIEHGADIRAQDSLGNTVLHIlVLQPNKTFACQM 188
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 78-341 8.30e-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: 8.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145    78 PDRENVSLLHWAAINNRL----ELVKFYISKGAVIDQLggdlnstpLHwAIRQGHLPMVILLLQH--------GADPTLI 145
Cdd:TIGR00870  48 PDRLGRSALFVAAIENENleltELLLNLSCRGAVGDTL--------LH-AISLEYVDAVEAILLHllaafrksGPLELAN 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145   146 D------GEGFSSIHLAVLFQHMPIIAYLISKGQSVN------------MTDVNGQTPLMLSAYKVIG-PEPTGFLLKFN 206
Cdd:TIGR00870 119 DqytsefTPGITALHLAAHRQNYEIVKLLLERGASVParacgdffvksqGVDSFYHGESPLNAAACLGsPSIVALLSEDP 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145   207 PSLSVVDKThQNTPLHWAV-----AAGN-----------VSAVDKLLEAGSSLDIRNAKGETPLDMA-LQSKNQLISHML 269
Cdd:TIGR00870 199 ADILTADSL-GNTLLHLLVmenefKAEYeelscqmynfaLSLLDKLRDSKELEVILNHQGLTPLKLAaKEGRIVLFRLKL 277

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27229145   270 RTEAKmraNKQFRLWRWlhkCELFLLLIlsmitlWAVGyiLD-FNSDSWLLKgclLVALFFLTSLFPRFLVGY 341
Cdd:TIGR00870 278 AIKYK---QKKFVAWPN---GQQLLSLY------WLEE--LDgWRRKQSVLE---LIVVFVIGLKFPELSDMY 333
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
30-289 2.26e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 143.56  E-value: 2.26e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145  30 HENKELAKAKEILPLIEDSSNCDIVKATQYGIFERCKELVEAGYDVRQPDRENVSLLHWAAINNRLELVKFYISKGAVID 109
Cdd:COG0666  35 LLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVN 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145 110 QLGGDlNSTPLHWAIRQGHLPMVILLLQHGADPTLIDGEGFSSIHLAVLFQHMPIIAYLISKGQSVNMTDVNGqtplmls 189
Cdd:COG0666 115 ARDKD-GETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDG------- 186

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145 190 aykvigpeptgfllkfnpslsvvdkthqNTPLHWAVAAGNVSAVDKLLEAGSSLDIRNAKGETPLDMALQSKNQLISHML 269
Cdd:COG0666 187 ----------------------------ETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLL 238

                       250       260
                ....*....|....*....|
gi 27229145 270 RTEAKMRANKQFRLWRWLHK 289
Cdd:COG0666 239 LEAGADLNAKDKDGLTALLL 258
DHHC pfam01529
DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which ...
 423-557 5.03e-33

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: 123.25  E-value: 5.03e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145   423 DFRTFCTSCLIRKPLRSLHCHVCNSCVARFDQHCFWTGRCIGFGNHHHYIFFLLSLSMVCDWIIYGSFVYWSNHCATTFK 502
Cdd:pfam01529   3 DELKYCSTCNIYKPPRSKHCRVCNRCVLRFDHHCPWLNNCIGKRNHKYFILFLLYLTLYLILYLVLSLYYLVKLIESSTL 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 27229145   503 EDGLWTYLNQivacspWVLYIFMLAAFHFSWSTFLLINQLFQIaFLGLTSHERIS 557
Cdd:pfam01529  83 FFFLILFLFS------ISIILLILSLFFLLFLGILLFFHLYLI-SRNLTTYEFMK 130
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
56-192 6.39e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 116.59  E-value: 6.39e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145  56 ATQYGIFERCKELVEAGYDVRQPDRENVSLLHWAAINNRLELVKFYISKGAVIDQLGGDlNSTPLHWAIRQGHLPMVILL 135
Cdd:COG0666 127 AAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDND-GETPLHLAAENGHLEIVKLL 205

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 27229145 136 LQHGADPTLIDGEGFSSIHLAVLFQHMPIIAYLISKGQSVNMTDVNGQTPLMLSAYK 192
Cdd:COG0666 206 LEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAA 262
COG5273 COG5273
Uncharacterized protein containing DHHC-type Zn finger [General function prediction only];
341-588 1.16e-27

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


Pssm-ID: 227598 [Multi-domain]  Cd Length: 309  Bit Score: 113.69  E-value: 1.16e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145 341 YKNLVYLPTVFLLSSIFWIFMTwFILFFPDTAGSPLYFAFIFSIMAFLYFFYKTwaTDPGF--TKASEEERKVNIVTLAE 418
Cdd:COG5273  26 YAYKMFIGLFLLSRIVVYTLLV-IVKSLSLVVLFIILFIVILVLASFSYLLLLV--SDPGYlgENITLSGYRETISRLLD 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145 419 TGSLDFRTFCTSCLIRKPLRSLHCHVCNSCVARFDQHCFWTGRCIGFGNHHHYIFFLLslsmvcdWIIYGSFVYWSNHCA 498
Cdd:COG5273 103 DGKFGTENFCSTCNIYKPPRSHHCSICNRCVLKFDHHCPWINNCVGFRNYRFFYQFLL-------YTILVALVVLLSTAY 175

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145 499 TTFKEDGLWTYLNQIV-------ACSPWVLYIFMLAAFHFswSTFLLINQLFQIAFL----GLTSHERISLLKQS-RHMK 566
Cdd:COG5273 176 YIAGIFSIRHDTSLAIcflifgcSLLGVVFFIITTLLLLF--LIYLILNNLTTIEFIqisrGGSTLEFFPLCRESnLPFT 253

                       250       260
                ....*....|....*....|....
gi 27229145 567 QTLSLRKT--PYNLGFTQNLADFF 588
Cdd:COG5273 254 NIFDSSEGalPLDLGIGQNLSTIK 277
Ank_2 pfam12796
Ankyrin repeats (3 copies);
56-146 3.33e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.77  E-value: 3.33e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145    56 ATQYGIFERCKELVEAGYDVRQPDRENVSLLHWAAINNRLELVKFYISKGAVIDQLGGDlnsTPLHWAIRQGHLPMVILL 135
Cdd:pfam12796   4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR---TALHYAARSGHLEIVKLL 80

                          90
                  ....*....|.
gi 27229145   136 LQHGADPTLID 146
Cdd:pfam12796  81 LEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
86-179 1.58e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.85  E-value: 1.58e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145    86 LHWAAINNRLELVKFYISKGAVIDQLGGDlNSTPLHWAIRQGHLPMVILLLQHGAdpTLIDGEGFSSIHLAVLFQHMPII 165
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKN-GRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIV 77

                          90
                  ....*....|....
gi 27229145   166 AYLISKGQSVNMTD 179
Cdd:pfam12796  78 KLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 66-269 5.71e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 83.56  E-value: 5.71e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145   66 KELVEAGYDVRQPDRENVSLLHWAA-----INNRLELVKFYISKGAVIDQlGGDLNSTPLHWAI--RQGHLPMVILLLQH 138
Cdd:PHA03100  52 KILLDNGADINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLEYGANVNA-PDNNGITPLLYAIskKSNSYSIVEYLLDN 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145  139 GADPTLIDGEGFSSIHLAVLFQH--MPIIAYLISKGQSVN-MTDVNgqtplmlsaykvigpeptgFLLKFNPSLSVVDKt 215
Cdd:PHA03100 131 GANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINaKNRVN-------------------YLLSYGVPINIKDV- 190

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 27229145  216 HQNTPLHWAVAAGNVSAVDKLLEAGSSLDIRNAKGETPLDMALQSKNQLISHML 269
Cdd:PHA03100 191 YGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLL 244
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
56-186 8.66e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 81.15  E-value: 8.66e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145  56 ATQYGIFERCKELVEAGYDVRQPDRENVSLLHWAAINNRLELVKFYISKGAVIDQLGGDLNsTPLHWAIRQGHLPMVILL 135
Cdd:COG0666 160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGK-TALDLAAENGNLEIVKLL 238

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 27229145 136 LQHGADPTLIDGEGFSSIHLAVLFQHMPIIAYLISKGQSVNMTDVNGQTPL 186
Cdd:COG0666 239 LEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 63-264 1.31e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 82.70  E-value: 1.31e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145   63 ERCKELVEAGYDVRQPDRENVSLLHWAAINNRLELVKFYISKGAVIDqLGGDLNSTPLHWAIRQGHLPMVILLLQHGADP 142
Cdd:PHA02874 105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVN-IEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYA 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145  143 TLIDGEGFSSIHLAVLFQHMPIIAYLISKGQSVNMTDVNGQTPLMLSaykVIGPEPTGFLLKFNPSLSVVDkTHQNTPLH 222
Cdd:PHA02874 184 NVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA---IIHNRSAIELLINNASINDQD-IDGSTPLH 259

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 27229145  223 WAVA-AGNVSAVDKLLEAGSSLDIRNAKGETPLDMALQSKNQL 264
Cdd:PHA02874 260 HAINpPCDIDIIDILLYHKADISIKDNKGENPIDTAFKYINKD 302
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 25-271 2.15e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 82.80  E-value: 2.15e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145   25 HGICVHENkelakAKEILplIEDSSNCDIVKATQYG--------IFERCKELVE---AGYDVRQpDRENVSLLHWAAINN 93
Cdd:PHA02876  80 HTICIIPN-----VMDIV--ISLTLDCDIILDIKYAsiilnkhkLDEACIHILKeaiSGNDIHY-DKINESIEYMKLIKE 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145   94 RLELVKFYISKgaVIDQLGGDLNS------TPLHWAIRQGHLPMVILLLQHGADPTLIDGEGFSSIHLAVLFQHMPIIAY 167
Cdd:PHA02876 152 RIQQDELLIAE--MLLEGGADVNAkdiyciTPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKA 229

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145  168 LISKGQSVNMTDVNgqtplMLSAYKVIGPEPTGFLLKFNPSLSVVDkTHQNTPLHWAVAAGNVSA-VDKLLEAGSSLDIR 246
Cdd:PHA02876 230 IIDNRSNINKNDLS-----LLKAIRNEDLETSLLLYDAGFSVNSID-DCKNTPLHHASQAPSLSRlVPKLLERGADVNAK 303

                        250       260
                 ....*....|....*....|....*
gi 27229145  247 NAKGETPLdmALQSKNQLISHMLRT 271
Cdd:PHA02876 304 NIKGETPL--YLMAKNGYDTENIRT 326
PHA03095 PHA03095
ankyrin-like protein; Provisional
 68-262 2.32e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 81.99  E-value: 2.32e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145   68 LVEAGYDVRQPDRENVSLLHWAAIN-NRLELVKFYISKGAVIDQlGGDLNSTPLH------WAirqgHLPMVILLLQHGA 140
Cdd:PHA03095  69 LLEAGADVNAPERCGFTPLHLYLYNaTTLDVIKLLIKAGADVNA-KDKVGRTPLHvylsgfNI----NPKVIRLLLRKGA 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145  141 DPTLIDGEGFSSIHLAVLFQHMPI--IAYLISKGQSVNMTDVNGQTPL--MLSAYK----------VIGPEPTGFLLKFN 206
Cdd:PHA03095 144 DVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADVYAVDDRFRSLLhhHLQSFKprarivreliRAGCDPAATDMLGN 223

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27229145  207 PSLSV---------------------VDKTHQN--TPLHWAVAAGNVSAVDKLLEAGSSLDIRNAKGETPLDMALQSKN 262
Cdd:PHA03095 224 TPLHSmatgssckrslvlplliagisINARNRYgqTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNN 302
PHA03095 PHA03095
ankyrin-like protein; Provisional
 92-260 2.19e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 78.91  E-value: 2.19e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145   92 NNRLELVKFYISKGAVIDQLGGdLNSTPLHWAIRQGHLP---MVILLLQHGADPTLIDGEGFSSIHLAVLFQH-MPIIAY 167
Cdd:PHA03095  24 NVTVEEVRRLLAAGADVNFRGE-YGKTPLHLYLHYSSEKvkdIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKL 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145  168 LISKGQSVNMTDVNGQTPlmLSAY---KVIGPEPTGFLLKFNPSLSVVDKtHQNTPLHWAVAAGNVSA--VDKLLEAGSS 242
Cdd:PHA03095 103 LIKAGADVNAKDKVGRTP--LHVYlsgFNINPKVIRLLLRKGADVNALDL-YGMTPLAVLLKSRNANVelLRLLIDAGAD 179

                        170
                 ....*....|....*...
gi 27229145  243 LDIRNAKGETPLDMALQS 260
Cdd:PHA03095 180 VYAVDDRFRSLLHHHLQS 197
Ank_2 pfam12796
Ankyrin repeats (3 copies);
120-247 1.16e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 69.76  E-value: 1.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145   120 LHWAIRQGHLPMVILLLQHGADPTLIDGEGFSSIHLAVLFQHMPIIAYLISKGQsVNMTDvngqtplmlsaykvigpept 199
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD-VNLKD-------------------- 59

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 27229145   200 gfllkfnpslsvvdktHQNTPLHWAVAAGNVSAVDKLLEAGSSLDIRN 247
Cdd:pfam12796  60 ----------------NGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 96-268 3.56e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 68.75  E-value: 3.56e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145   96 ELVKFYISKGAVIDQLGGDLNSTPLHWAIRQGHLPMVILLLQHGADPTLIDGEGFSSIHLAVLFQHMPIIAYLISKGQSV 175
Cdd:PHA02878 148 EITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAST 227

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145  176 NMTDVNGQTPLMLSAYKVIGPEPTGFLLKFNPSLSVVDKTHQNTPLHWAVAAGNVSAVdkLLEAGSSLDIRNAKGETPLD 255
Cdd:PHA02878 228 DARDKCGNTPLHISVGYCKDYDILKLLLEHGVDVNAKSYILGLTALHSSIKSERKLKL--LLEYGADINSLNSYKLTPLS 305

                        170
                 ....*....|....*....
gi 27229145  256 MALQSK------NQLISHM 268
Cdd:PHA02878 306 SAVKQYlcinigRILISNI 324
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 74-245 2.93e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 62.70  E-value: 2.93e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145   74 DVRQPDREnvSLLHWAAINNRLELVKFYISKGAVIDQLGGDLNSTPLHWAIRQGHLPMVILLLQHGADPTLIDGEGFSSI 153
Cdd:PHA02875  62 DVKYPDIE--SELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPL 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145  154 HLAVLFQHMPIIAYLISKGQSVNMTDVNGQTPLMLS-AYKVIgpEPTGFLLKFNPSLSVVDKTHQNTPLHWAVAAGNVSA 232
Cdd:PHA02875 140 HLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAmAKGDI--AICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDI 217

                        170
                 ....*....|...
gi 27229145  233 VDKLLEAGSSLDI 245
Cdd:PHA02875 218 VRLFIKRGADCNI 230
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 66-225 4.59e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 62.20  E-value: 4.59e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145   66 KELVEAGYDVRQPDRENV-SLLHWAAINNRLELVKFYISKGAVIDQLgGDLNSTPLHWAIRQGHLPMVILLLQHGADPTL 144
Cdd:PHA02878 151 KLLLSYGADINMKDRHKGnTALHYATENKDQRLTELLLSYGANVNIP-DKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145  145 IDGEGFSSIHLAVLF-QHMPIIAYLISKGQSVNM-TDVNGQTPLMLSaykVIGPEPTGFLLKFNPSLSVVDkTHQNTPLH 222
Cdd:PHA02878 230 RDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAkSYILGLTALHSS---IKSERKLKLLLEYGADINSLN-SYKLTPLS 305


                 ...
gi 27229145  223 WAV 225
Cdd:PHA02878 306 SAV 308
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 118-269 9.31e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.16  E-value: 9.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145  118 TPLHWAIRQGHLPMVILLLQHGADPTLIDGEGFSSIHLAVLFQHMPIIAYLISKGQSVNmtDV---NGQTPLMLsAYKVI 194
Cdd:PHA02875  37 SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAD--DVfykDGMTPLHL-ATILK 113

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27229145  195 GPEPTGFLLKF--NPSLSVVDKThqnTPLHWAVAAGNVSAVDKLLEAGSSLDIRNAKGETPLDMALQSKNQLISHML 269
Cdd:PHA02875 114 KLDIMKLLIARgaDPDIPNTDKF---SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKML 187
Ank_4 pfam13637
Ankyrin repeats (many copies);
116-169 3.69e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.66  E-value: 3.69e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 27229145   116 NSTPLHWAIRQGHLPMVILLLQHGADPTLIDGEGFSSIHLAVLFQHMPIIAYLI 169
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 56-269 5.28e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 59.31  E-value: 5.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145   56 ATQYGIFERCKELVEAGYDVRQPDRENVSLLHWAAINNRLELVKFYISKGAVIDQlggdlNSTPLHWAIRQGHLPMVILL 135
Cdd:PHA02876 185 AAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINK-----NDLSLLKAIRNEDLETSLLL 259

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145  136 LQHGADPTLIDGEGFSSIHLAVLFQHMP-IIAYLISKGQSVNMTDVNGQTPLMLSAYKVIGPEPTGFLLKFNPSLSVVDK 214
Cdd:PHA02876 260 YDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGYDTENIRTLIMLGADVNAADR 339

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 27229145  215 THqNTPLHWAVAAG-NVSAVDKLLEAGSSLDIRNAKGETPLDMALQSKNQLISHML 269
Cdd:PHA02876 340 LY-ITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTL 394
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 66-179 7.27e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 58.14  E-value: 7.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145   66 KELVEAGYDVRQPDRENVSLLHWAAINNR--LELVKFYISKGAVIDQ---------LGGDLNS------TPLHWAIRQGH 128
Cdd:PHA03100 125 EYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAknrvnyllsYGVPINIkdvygfTPLHYAVYNNN 204

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 27229145  129 LPMVILLLQHGADPTLIDGEGFSSIHLAVLFQHMPIIAYLISKGQSVNMTD 179
Cdd:PHA03100 205 PEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTII 255
Ank_4 pfam13637
Ankyrin repeats (many copies);
82-136 1.50e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.12  E-value: 1.50e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 27229145    82 NVSLLHWAAINNRLELVKFYISKGAVIDQLGGDLNsTPLHWAIRQGHLPMVILLL 136
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGE-TALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
202-257 1.33e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.50  E-value: 1.33e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 27229145   202 LLKFNPSLSVVDKTHQNTPLHWAVAAGNVSAVDKLLEAGSSLDIRNAKGETPLDMA 257
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
101-156 4.03e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.96  E-value: 4.03e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 27229145   101 YISKGAVIDQLGGDLNSTPLHWAIRQGHLPMVILLLQHGADPTLIDGEGFSSIHLA 156
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 118-146 7.49e-06

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: 43.05  E-value: 7.49e-06
                          10        20        30
                  ....*....|....*....|....*....|
gi 27229145   118 TPLHWAI-RQGHLPMVILLLQHGADPTLID 146
Cdd:pfam00023   4 TPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 63-243 8.87e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.91  E-value: 8.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145   63 ERCKELVEAGYDVRQPDRENVSLLHWAAINNRlelvkfyiSKGAVID--QLGGDLNS------TPLHWAIRQGHLPMVIL 134
Cdd:PHA02876 322 ENIRTLIMLGADVNAADRLYITPLHQASTLDR--------NKDIVITllELGANVNArdycdkTPIHYAAVRNNVVIINT 393

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145  135 LLQHGADPTLIDGEGFSSIHLAvLFQHMPIIAY--LISKGQSVNMTDVNGQTPLMLSAYKVIGPEPTGFLLKFNPSLSVV 212
Cdd:PHA02876 394 LLDYGADIEALSQKIGTALHFA-LCGTNPYMSVktLIDRGANVNSKNKDLSTPLHYACKKNCKLDVIEMLLDNGADVNAI 472

                        170       180       190
                 ....*....|....*....|....*....|.
gi 27229145  213 DKTHQnTPLhwAVAAGNVSAVDKLLEAGSSL 243
Cdd:PHA02876 473 NIQNQ-YPL--LIALEYHGIVNILLHYGAEL 500
Ank_4 pfam13637
Ankyrin repeats (many copies);
217-262 1.31e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.65  E-value: 1.31e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 27229145   217 QNTPLHWAVAAGNVSAVDKLLEAGSSLDIRNAKGETPLDMALQSKN 262
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGN 46
PHA02798 PHA02798
ankyrin-like protein; Provisional
 27-176 2.43e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 47.14  E-value: 2.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145   27 ICVHENKELAKAKEILpliedsSNCDI-VKATQYGIFER-----------CKELVEAGYDVRQPDRENVS-----LLHWA 89
Cdd:PHA02798  10 ITFSDNVKLSTVKLLI------KSCNPnEIVNEYSIFQKylqrdspstdiVKLFINLGANVNGLDNEYSTplctiLSNIK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145   90 AINNRLELVKFYISKGAVIDQLGGDLNsTPLHWAIRQGH---LPMVILLLQHGADPTLIDGEGFSSIHLAVLFQH---MP 163
Cdd:PHA02798  84 DYKHMLDIVKILIENGADINKKNSDGE-TPLYCLLSNGYinnLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHhidIE 162

                        170
                 ....*....|...
gi 27229145  164 IIAYLISKGQSVN 176
Cdd:PHA02798 163 IIKLLLEKGVDIN 175
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 118-144 2.63e-05

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: 41.42  E-value: 2.63e-05
                           10        20
                   ....*....|....*....|....*..
gi 27229145    118 TPLHWAIRQGHLPMVILLLQHGADPTL 144
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 112-157 2.72e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.20  E-value: 2.72e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 27229145  112 GGDLNS------TPLHWAIRQGHLPMVILLLQHGADPTLIDGEGFSSIHLAV 157
Cdd:PTZ00322 105 GADPNCrdydgrTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAE 156
Ank_5 pfam13857
Ankyrin repeats (many copies);
135-186 3.21e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 3.21e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 27229145   135 LLQHG-ADPTLIDGEGFSSIHLAVLFQHMPIIAYLISKGQSVNMTDVNGQTPL 186
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 95-258 5.26e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 46.11  E-value: 5.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145   95 LELVKFYI-SKGAVIDqLGGDLNSTPLHWAIRQGHLPMVILLLQHGAD----------PTLI------------------ 145
Cdd:PHA02874  14 IEAIEKIIkNKGNCIN-ISVDETTTPLIDAIRSGDAKIVELFIKHGADinhintkiphPLLTaikigahdiikllidngv 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145  146 ----------------------------DGEGFSSIHLAVLFQHMPIIAYLISKGQSVNMTDVNGQTPLMLS----AYKV 193
Cdd:PHA02874  93 dtsilpipciekdmiktildcgidvnikDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAikhnFFDI 172

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27229145  194 IGpeptgfLLKFNPSLSVVDKTHQNTPLHWAVAAGNVSAVDKLLEAGSSLDIRNAKGETPLDMAL 258
Cdd:PHA02874 173 IK------LLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI 231
Ank_2 pfam12796
Ankyrin repeats (3 copies);
221-290 7.98e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 41.64  E-value: 7.98e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27229145   221 LHWAVAAGNVSAVDKLLEAGSSLDIRNAKGETPLDMALQSKN-QLISHMLrteAKMRANKQFRLWRWLHKC 290
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHlEIVKLLL---EHADVNLKDNGRTALHYA 68
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 64-141 1.13e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 45.04  E-value: 1.13e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27229145   64 RCKELVEAGYDVRQPDRENVSLLHWAAINNRLELVKFYISKGAVIDqLGGDLNSTPLHWAIRQGHLPMVILLLQHGAD 141
Cdd:PHA03100 174 RVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPN-LVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
PHA02798 PHA02798
ankyrin-like protein; Provisional
 68-265 1.27e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 44.83  E-value: 1.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145   68 LVEAGYDVRQPDRENVS----LLHWAAINNrLELVKFYISKGAVIDQLGGDlNSTPLHWAIRQGH---LPMVILLLQHGA 140
Cdd:PHA02798  95 LIENGADINKKNSDGETplycLLSNGYINN-LEILLFMIENGADTTLLDKD-GFTMLQVYLQSNHhidIEIIKLLLEKGV 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145  141 DPTLIDG-EGFSSIHLAVLFQ----HMPIIAYLISKGQSVNMTDVNGQTPLM------LSAYKVIGPEPTGFLLKFnpsL 209
Cdd:PHA02798 173 DINTHNNkEKYDTLHCYFKYNidriDADILKLFVDNGFIINKENKSHKKKFMeylnslLYDNKRFKKNILDFIFSY---I 249

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 27229145  210 SVVDKTHQN-TPLHWAVAAGNVSAVDKLLEAGSSLDIRNAKGETPLDMALQSKNQLI 265
Cdd:PHA02798 250 DINQVDELGfNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFI 306
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 77-268 1.33e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 45.00  E-value: 1.33e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145  77 QPDRENVSLLHWAAINNRLELVKfYISKGAVIDQLG-GDLNSTPLHWAIRQGHLPMVILLLQhgADPTLIDG-------E 148
Cdd:cd22192  12 QQKRISESPLLLAAKENDVQAIK-KLLKCPSCDLFQrGALGETALHVAALYDNLEAAVVLME--AAPELVNEpmtsdlyQ 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145 149 GFSSIHLAVLFQHMPIIAYLISKGQSVnmtdvngqtplmlsaykvIGPEPTGFLLKFNPSLSVVDKTHqntPLHWAVAAG 228
Cdd:cd22192  89 GETALHIAVVNQNLNLVRELIARGADV------------------VSPRATGTFFRPGPKNLIYYGEH---PLSFAACVG 147

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 27229145 229 NVSAVDKLLEAGSSLDIRNAKGETPLDM-ALQSKNQLISHM 268
Cdd:cd22192 148 NEEIVRLLIEHGADIRAQDSLGNTVLHIlVLQPNKTFACQM 188
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 118-142 1.50e-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: 39.16  E-value: 1.50e-04
                          10        20
                  ....*....|....*....|....*
gi 27229145   118 TPLHWAIRQGHLPMVILLLQHGADP 142
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADI 28
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 216-247 2.92e-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. 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: 38.42  E-value: 2.92e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 27229145   216 HQNTPLHWAVA-AGNVSAVDKLLEAGSSLDIRN 247
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 119-269 5.65e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 42.95  E-value: 5.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145  119 PLHWAIRQGHLPMVILLLQHGADPTLIDGEGFSSIHLAVLFQHMPIIAYLISK-------------GQSVNMTDVNGQTP 185
Cdd:PHA02878  40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSinkcsvfytlvaiKDAFNNRNVEIFKI 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145  186 LMLSAYK-----------------VIGPEPTGFLLKFNPSLSVVDKTHQNTPLHWAVAAGNVSAVDKLLEAGSSLDIRNA 248
Cdd:PHA02878 120 ILTNRYKniqtidlvyidkkskddIIEAEITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDK 199

                        170       180
                 ....*....|....*....|.
gi 27229145  249 KGETPLDMALQSKNQLISHML 269
Cdd:PHA02878 200 TNNSPLHHAVKHYNKPIVHIL 220
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 134-189 8.43e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.58  E-value: 8.43e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 27229145  134 LLLQHGADPTLIDGEGFSSIHLAVLFQHMPIIAYLISKGQSVNMTDVNGQTPLMLS 189
Cdd:PTZ00322 100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA 155
PHA03095 PHA03095
ankyrin-like protein; Provisional
 66-171 1.57e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 41.55  E-value: 1.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145   66 KELVEAGYDVRQPDRENVSLLHWAAINN--RLELVKFYISKGAVIDQLgGDLNSTPLHWAIRQGHLPMVILLLQHGADPT 143
Cdd:PHA03095 206 RELIRAGCDPAATDMLGNTPLHSMATGSscKRSLVLPLLIAGISINAR-NRYGQTPLHYAAVFNNPRACRRLIALGADIN 284

                         90       100
                 ....*....|....*....|....*...
gi 27229145  144 LIDGEGFSSIHLAVLFQHMPIIAYLISK 171
Cdd:PHA03095 285 AVSSDGNTPLSLMVRNNNGRAVRAALAK 312
Ank_4 pfam13637
Ankyrin repeats (many copies);
151-192 2.06e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.48  E-value: 2.06e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 27229145   151 SSIHLAVLFQHMPIIAYLISKGQSVNMTDVNGQTPLMLSAYK 192
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASN 44
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 114-256 2.20e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 39.80  E-value: 2.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145  114 DLNSTPLHWAIRQGH--LPMVILLLQHGADPT-LIDGEGFSSIHLAVLFQ---HMPIIAYLISKGQSVNMTDVNGQTPLM 187
Cdd:PHA02859  49 DLYETPIFSCLEKDKvnVEILKFLIENGADVNfKTRDNNLSALHHYLSFNknvEPEILKILIDSGSSITEEDEDGKNLLH 128

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27229145  188 LSAYKV-IGPEPTGFLLKFNPSLSVVDKtHQNTPLH-WAVAAGNVSAVDKLLEAGSSLDIRNAKGETPLDM 256
Cdd:PHA02859 129 MYMCNFnVRINVIKLLIDSGVSFLNKDF-DNNNILYsYILFHSDKKIFDFLTSLGIDINETNKSGYNCYDL 198
PHA02946 PHA02946
ankyin-like protein; Provisional
 30-271 2.24e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 40.81  E-value: 2.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145   30 HENKELAKAKEILPLIEDSSNCDIVKA--TQYGIFER-CKELVEAGYDVRQPDRENVSLLHWAAINNRLELVKFYISKGA 106
Cdd:PHA02946  17 YNSKNLDVFRNMLQAIEPSGNYHILHAycGIKGLDERfVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGA 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145  107 viDQLGGDL-NSTPLHW--AIRQGHLPMVILLLQHGAD-PTLIDGEGFSSIhLAVLFQHMPIIAYLISKGQSVNMTDVNG 182
Cdd:PHA02946  97 --DPNACDKqHKTPLYYlsGTDDEVIERINLLVQYGAKiNNSVDEEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFG 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145  183 QTPLMlsaYKVIGPEPTG----FLLKFNPSLSVVDKThQNTPLHWAVA--AGNVSAVDKLLEAgSSLDIRNAKGETPLDM 256
Cdd:PHA02946 174 KNHIH---RHLMSDNPKAstisWMMKLGISPSKPDHD-GNTPLHIVCSktVKNVDIINLLLPS-TDVNKQNKFGDSPLTL 248

                        250
                 ....*....|....*..
gi 27229145  257 ALQ--SKNQLISHMLRT 271
Cdd:PHA02946 249 LIKtlSPAHLINKLLST 265
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 216-245 2.88e-03

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: 35.64  E-value: 2.88e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 27229145    216 HQNTPLHWAVAAGNVSAVDKLLEAGSSLDI 245
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 118-265 6.46e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 39.47  E-value: 6.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145  118 TPLHWAIRQGHLPMVILLLQHGADPTLIDGEGFSSIHLAVLFQHMPIIAYLIskgQSVNMTDVNGQTPLMLSAYKVIGPE 197
Cdd:PLN03192 560 TPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY---HFASISDPHAAGDLLCTAAKRNDLT 636

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27229145  198 PTGFLLKFnpSLSVVDKTHQN-TPLHWAVAAGNVSAVDKLLEAGSSLDirnaKGETPLDMALQSKNQLI 265
Cdd:PLN03192 637 AMKELLKQ--GLNVDSEDHQGaTALQVAMAEDHVDMVRLLIMNGADVD----KANTDDDFSPTELRELL 699
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 216-269 6.66e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 39.50  E-value: 6.66e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 27229145  216 HQNTPLHWAVAAGNVSAVDKLLEAGSSLDIRNAKGETPLDMALQSKNQLISHML 269
Cdd:PTZ00322 114 DGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 78-341 8.30e-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: 8.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145    78 PDRENVSLLHWAAINNRL----ELVKFYISKGAVIDQLggdlnstpLHwAIRQGHLPMVILLLQH--------GADPTLI 145
Cdd:TIGR00870  48 PDRLGRSALFVAAIENENleltELLLNLSCRGAVGDTL--------LH-AISLEYVDAVEAILLHllaafrksGPLELAN 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145   146 D------GEGFSSIHLAVLFQHMPIIAYLISKGQSVN------------MTDVNGQTPLMLSAYKVIG-PEPTGFLLKFN 206
Cdd:TIGR00870 119 DqytsefTPGITALHLAAHRQNYEIVKLLLERGASVParacgdffvksqGVDSFYHGESPLNAAACLGsPSIVALLSEDP 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229145   207 PSLSVVDKThQNTPLHWAV-----AAGN-----------VSAVDKLLEAGSSLDIRNAKGETPLDMA-LQSKNQLISHML 269
Cdd:TIGR00870 199 ADILTADSL-GNTLLHLLVmenefKAEYeelscqmynfaLSLLDKLRDSKELEVILNHQGLTPLKLAaKEGRIVLFRLKL 277

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27229145   270 RTEAKmraNKQFRLWRWlhkCELFLLLIlsmitlWAVGyiLD-FNSDSWLLKgclLVALFFLTSLFPRFLVGY 341
Cdd:TIGR00870 278 AIKYK---QKKFVAWPN---GQQLLSLY------WLEE--LDgWRRKQSVLE---LIVVFVIGLKFPELSDMY 333
 
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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