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Conserved domains on  [gi|2217283422|ref|XP_047283094|]
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palmitoyltransferase ZDHHC13 isoform X1 [Homo sapiens]

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];
49-290 2.11e-39

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 146.64  E-value: 2.11e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422  49 AHENKELANAREALPLIEDSSNCDIVKATQYGIFERCKELVEAGYDVRQPDKENVSLLHWAAINNRLDLVKFYISKGAVV 128
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422 129 DQLGGDLNsTPLHWAIRQGHLPMVILLLQHGADPTLIDGEGFSSIHLAVLFQHMPIIAYLISKGQSVNMTDVNGQTPLML 208
Cdd:COG0666    81 NAKDDGGN-TLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422 209 SAHKviG-PEPTGFLLKFNPSLNVVDKiHQNTPLHWAVAAGNVNAVDKLLEAGSSLDIQNVKGETPLDMALQNKNQLIIH 287
Cdd:COG0666   160 AAAN--GnLEIVKLLLEAGADVNARDN-DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVK 236


                  ...
gi 2217283422 288 MLK 290
Cdd:COG0666   237 LLL 239
DHHC pfam01529
DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which ...
 443-579 4.46e-34

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: 126.33  E-value: 4.46e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422 443 DFRTFCTSCLIRKPLRSLHCHVCNCCVARYDQHCLWTGRCIGFGNHHYYIFFLFFLSMVCGWIIYGSFIYLSSHCATTFK 522
Cdd:pfam01529   3 DELKYCSTCNIYKPPRSKHCRVCNRCVLRFDHHCPWLNNCIGKRNHKYFILFLLYLTLYLILYLVLSLYYLVKLIESSTL 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2217283422 523 EDGLWTYLNQivacspWVLYILMLATFHFSWSTFLLLNQLFQIaFLGLTSHERISLQ 579
Cdd:pfam01529  83 FFFLILFLFS------ISIILLILSLFFLLFLGILLFFHLYLI-SRNLTTYEFMKKK 132
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
49-290 2.11e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 146.64  E-value: 2.11e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422  49 AHENKELANAREALPLIEDSSNCDIVKATQYGIFERCKELVEAGYDVRQPDKENVSLLHWAAINNRLDLVKFYISKGAVV 128
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422 129 DQLGGDLNsTPLHWAIRQGHLPMVILLLQHGADPTLIDGEGFSSIHLAVLFQHMPIIAYLISKGQSVNMTDVNGQTPLML 208
Cdd:COG0666    81 NAKDDGGN-TLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422 209 SAHKviG-PEPTGFLLKFNPSLNVVDKiHQNTPLHWAVAAGNVNAVDKLLEAGSSLDIQNVKGETPLDMALQNKNQLIIH 287
Cdd:COG0666   160 AAAN--GnLEIVKLLLEAGADVNARDN-DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVK 236


                  ...
gi 2217283422 288 MLK 290
Cdd:COG0666   237 LLL 239
DHHC pfam01529
DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which ...
 443-579 4.46e-34

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: 126.33  E-value: 4.46e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422 443 DFRTFCTSCLIRKPLRSLHCHVCNCCVARYDQHCLWTGRCIGFGNHHYYIFFLFFLSMVCGWIIYGSFIYLSSHCATTFK 522
Cdd:pfam01529   3 DELKYCSTCNIYKPPRSKHCRVCNRCVLRFDHHCPWLNNCIGKRNHKYFILFLLYLTLYLILYLVLSLYYLVKLIESSTL 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2217283422 523 EDGLWTYLNQivacspWVLYILMLATFHFSWSTFLLLNQLFQIaFLGLTSHERISLQ 579
Cdd:pfam01529  83 FFFLILFLFS------ISIILLILSLFFLLFLGILLFFHLYLI-SRNLTTYEFMKKK 132
COG5273 COG5273
Uncharacterized protein containing DHHC-type Zn finger [General function prediction only];
361-608 4.35e-26

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


Pssm-ID: 227598 [Multi-domain]  Cd Length: 309  Bit Score: 109.07  E-value: 4.35e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422 361 YKNLVYLPTAFLLSSVFWIFMTwFILFFPDLAGAPFYFSFIFSIVAFLYFFYKTwaTDPGFTKASEEEKKVN--IITLAE 438
Cdd:COG5273    26 YAYKMFIGLFLLSRIVVYTLLV-IVKSLSLVVLFIILFIVILVLASFSYLLLLV--SDPGYLGENITLSGYRetISRLLD 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422 439 TGSLDFRTFCTSCLIRKPLRSLHCHVCNCCVARYDQHCLWTGRCIGFGNHHYYIFFLFFLSMVcgwIIYgSFIYLSSHCA 518
Cdd:COG5273   103 DGKFGTENFCSTCNIYKPPRSHHCSICNRCVLKFDHHCPWINNCVGFRNYRFFYQFLLYTILV---ALV-VLLSTAYYIA 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422 519 TTFKEDGLWTYLNQIVACSPWVLYILMLATFHFSW--STFLLLNQLFQIAFL-----GLTSHERISLQKQSKHMKQTLSL 591
Cdd:COG5273   179 GIFSIRHDTSLAICFLIFGCSLLGVVFFIITTLLLlfLIYLILNNLTTIEFIqisrgGSTLEFFPLCRESNLPFTNIFDS 258

                         250
                  ....*....|....*....
gi 2217283422 592 RKT--PYNLGFMQNLADFF 608
Cdd:COG5273   259 SEGalPLDLGIGQNLSTIK 277
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 86-289 2.64e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 90.88  E-value: 2.64e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422  86 KELVEAGYDVRQPDKENVSLLHWAA-----INNRLDLVKFYISKGAVVDQlGGDLNSTPLHWAI--RQGHLPMVILLLQH 158
Cdd:PHA03100   52 KILLDNGADINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLEYGANVNA-PDNNGITPLLYAIskKSNSYSIVEYLLDN 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422 159 GADPTLIDGEGFSSIHLAVLFQH--MPIIAYLISKGQSVN-MTDVNgqtplmlsahkvigpeptgFLLKFNPSLNVVDKI 235
Cdd:PHA03100  131 GANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINaKNRVN-------------------YLLSYGVPINIKDVY 191

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2217283422 236 HqNTPLHWAVAAGNVNAVDKLLEAGSSLDIQNVKGETPLDMALQNKNQLIIHML 289
Cdd:PHA03100  192 G-FTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLL 244
Ank_2 pfam12796
Ankyrin repeats (3 copies);
76-166 8.07e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 81.70  E-value: 8.07e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422  76 ATQYGIFERCKELVEAGYDVRQPDKENVSLLHWAAINNRLDLVKFYISKGAVVDQLGGDlnsTPLHWAIRQGHLPMVILL 155
Cdd:pfam12796   4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR---TALHYAARSGHLEIVKLL 80

                          90
                  ....*....|.
gi 2217283422 156 LQHGADPTLID 166
Cdd:pfam12796  81 LEKGADINVKD 91
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 138-164 2.25e-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: 2.25e-05
                           10        20
                   ....*....|....*....|....*..
gi 2217283422  138 TPLHWAIRQGHLPMVILLLQHGADPTL 164
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 104-288 3.15e-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: 43.85  E-value: 3.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422 104 SLLHWAAINNRLDLVKFYISKGAVVDQLGGDLNSTPLHWAIRQGHLPMVILLLQhgADPTLIDG-------EGFSSIHLA 176
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNEpmtsdlyQGETALHIA 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422 177 VLFQHMPIIAYLISKGQSVnmtdvngqtplmlsahkvIGPEPTGFLLKFNPSlnvvDKIHQNT-PLHWAVAAGNVNAVDK 255
Cdd:cd22192    97 VVNQNLNLVRELIARGADV------------------VSPRATGTFFRPGPK----NLIYYGEhPLSFAACVGNEEIVRL 154

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2217283422 256 LLEAGSSLDIQNVKGETPLDM-ALQNKNQLIIHM 288
Cdd:cd22192   155 LIEHGADIRAQDSLGNTVLHIlVLQPNKTFACQM 188
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
49-290 2.11e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 146.64  E-value: 2.11e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422  49 AHENKELANAREALPLIEDSSNCDIVKATQYGIFERCKELVEAGYDVRQPDKENVSLLHWAAINNRLDLVKFYISKGAVV 128
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422 129 DQLGGDLNsTPLHWAIRQGHLPMVILLLQHGADPTLIDGEGFSSIHLAVLFQHMPIIAYLISKGQSVNMTDVNGQTPLML 208
Cdd:COG0666    81 NAKDDGGN-TLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422 209 SAHKviG-PEPTGFLLKFNPSLNVVDKiHQNTPLHWAVAAGNVNAVDKLLEAGSSLDIQNVKGETPLDMALQNKNQLIIH 287
Cdd:COG0666   160 AAAN--GnLEIVKLLLEAGADVNARDN-DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVK 236


                  ...
gi 2217283422 288 MLK 290
Cdd:COG0666   237 LLL 239
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
49-300 2.93e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 146.25  E-value: 2.93e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422  49 AHENKELANAREALPLIEDSSNCDIVKATQYGIFERCKELVEAGYDVRQPDKENVSLLHWAAINNRLDLVKFYISKGAVV 128
Cdd:COG0666    34 LLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADV 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422 129 DQLGGDLNsTPLHWAIRQGHLPMVILLLQHGADPTLIDGEGFSSIHLAVLFQHMPIIAYLISKGQSVNMTDVNGQTPLML 208
Cdd:COG0666   114 NARDKDGE-TPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHL 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422 209 SAHKviG-PEPTGFLLKFNPSLNVVDKiHQNTPLHWAVAAGNVNAVDKLLEAGSSLDIQNVKGETPLDMALQNKNQLIIH 287
Cdd:COG0666   193 AAEN--GhLEIVKLLLEAGADVNAKDN-DGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVK 269

                         250
                  ....*....|...
gi 2217283422 288 MLKTEAKMRANQK 300
Cdd:COG0666   270 LLLLALLLLAAAL 282
DHHC pfam01529
DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which ...
 443-579 4.46e-34

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: 126.33  E-value: 4.46e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422 443 DFRTFCTSCLIRKPLRSLHCHVCNCCVARYDQHCLWTGRCIGFGNHHYYIFFLFFLSMVCGWIIYGSFIYLSSHCATTFK 522
Cdd:pfam01529   3 DELKYCSTCNIYKPPRSKHCRVCNRCVLRFDHHCPWLNNCIGKRNHKYFILFLLYLTLYLILYLVLSLYYLVKLIESSTL 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2217283422 523 EDGLWTYLNQivacspWVLYILMLATFHFSWSTFLLLNQLFQIaFLGLTSHERISLQ 579
Cdd:pfam01529  83 FFFLILFLFS------ISIILLILSLFFLLFLGILLFFHLYLI-SRNLTTYEFMKKK 132
COG5273 COG5273
Uncharacterized protein containing DHHC-type Zn finger [General function prediction only];
361-608 4.35e-26

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


Pssm-ID: 227598 [Multi-domain]  Cd Length: 309  Bit Score: 109.07  E-value: 4.35e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422 361 YKNLVYLPTAFLLSSVFWIFMTwFILFFPDLAGAPFYFSFIFSIVAFLYFFYKTwaTDPGFTKASEEEKKVN--IITLAE 438
Cdd:COG5273    26 YAYKMFIGLFLLSRIVVYTLLV-IVKSLSLVVLFIILFIVILVLASFSYLLLLV--SDPGYLGENITLSGYRetISRLLD 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422 439 TGSLDFRTFCTSCLIRKPLRSLHCHVCNCCVARYDQHCLWTGRCIGFGNHHYYIFFLFFLSMVcgwIIYgSFIYLSSHCA 518
Cdd:COG5273   103 DGKFGTENFCSTCNIYKPPRSHHCSICNRCVLKFDHHCPWINNCVGFRNYRFFYQFLLYTILV---ALV-VLLSTAYYIA 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422 519 TTFKEDGLWTYLNQIVACSPWVLYILMLATFHFSW--STFLLLNQLFQIAFL-----GLTSHERISLQKQSKHMKQTLSL 591
Cdd:COG5273   179 GIFSIRHDTSLAICFLIFGCSLLGVVFFIITTLLLlfLIYLILNNLTTIEFIqisrgGSTLEFFPLCRESNLPFTNIFDS 258

                         250
                  ....*....|....*....
gi 2217283422 592 RKT--PYNLGFMQNLADFF 608
Cdd:COG5273   259 SEGalPLDLGIGQNLSTIK 277
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 86-289 2.64e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 90.88  E-value: 2.64e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422  86 KELVEAGYDVRQPDKENVSLLHWAA-----INNRLDLVKFYISKGAVVDQlGGDLNSTPLHWAI--RQGHLPMVILLLQH 158
Cdd:PHA03100   52 KILLDNGADINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLEYGANVNA-PDNNGITPLLYAIskKSNSYSIVEYLLDN 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422 159 GADPTLIDGEGFSSIHLAVLFQH--MPIIAYLISKGQSVN-MTDVNgqtplmlsahkvigpeptgFLLKFNPSLNVVDKI 235
Cdd:PHA03100  131 GANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINaKNRVN-------------------YLLSYGVPINIKDVY 191

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2217283422 236 HqNTPLHWAVAAGNVNAVDKLLEAGSSLDIQNVKGETPLDMALQNKNQLIIHML 289
Cdd:PHA03100  192 G-FTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLL 244
Ank_2 pfam12796
Ankyrin repeats (3 copies);
76-166 8.07e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 81.70  E-value: 8.07e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422  76 ATQYGIFERCKELVEAGYDVRQPDKENVSLLHWAAINNRLDLVKFYISKGAVVDQLGGDlnsTPLHWAIRQGHLPMVILL 155
Cdd:pfam12796   4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR---TALHYAARSGHLEIVKLL 80

                          90
                  ....*....|.
gi 2217283422 156 LQHGADPTLID 166
Cdd:pfam12796  81 LEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
106-199 1.68e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.85  E-value: 1.68e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422 106 LHWAAINNRLDLVKFYISKGAVVDQLGGDlNSTPLHWAIRQGHLPMVILLLQHGAdpTLIDGEGFSSIHLAVLFQHMPII 185
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKN-GRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIV 77

                          90
                  ....*....|....
gi 2217283422 186 AYLISKGQSVNMTD 199
Cdd:pfam12796  78 KLLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 83-284 7.16e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 83.47  E-value: 7.16e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422  83 ERCKELVEAGYDVRQPDKENVSLLHWAAINNRLDLVKFYISKGAVVDqLGGDLNSTPLHWAIRQGHLPMVILLLQHGADP 162
Cdd:PHA02874  105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVN-IEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYA 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422 163 TLIDGEGFSSIHLAVLFQHMPIIAYLISKGQSVNMTDVNGQTPLmlsaHKVIGPEPTGF-LLKFNPSLNVVDkIHQNTPL 241
Cdd:PHA02874  184 NVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPL----HNAIIHNRSAIeLLINNASINDQD-IDGSTPL 258

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2217283422 242 HWAVA-AGNVNAVDKLLEAGSSLDIQNVKGETPLDMALQNKNQL 284
Cdd:PHA02874  259 HHAINpPCDIDIIDILLYHKADISIKDNKGENPIDTAFKYINKD 302
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
76-206 9.59e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 81.15  E-value: 9.59e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422  76 ATQYGIFERCKELVEAGYDVRQPDKENVSLLHWAAINNRLDLVKFYISKGAVVDQLGGDLNsTPLHWAIRQGHLPMVILL 155
Cdd:COG0666   160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGK-TALDLAAENGNLEIVKLL 238

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2217283422 156 LQHGADPTLIDGEGFSSIHLAVLFQHMPIIAYLISKGQSVNMTDVNGQTPL 206
Cdd:COG0666   239 LEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 64-280 2.26e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 82.80  E-value: 2.26e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422  64 LIEDSSNCDIVKATQYG--------IFERCKELVE---AGYDVRQpDKENVSLLHWAAINNRLDLVKFYISKgaVVDQLG 132
Cdd:PHA02876   92 VISLTLDCDIILDIKYAsiilnkhkLDEACIHILKeaiSGNDIHY-DKINESIEYMKLIKERIQQDELLIAE--MLLEGG 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422 133 GDLNS------TPLHWAIRQGHLPMVILLLQHGADPTLIDGEGFSSIHLAVLFQHMPIIAYLISKGQSVNMTDVNgqtpl 206
Cdd:PHA02876  169 ADVNAkdiyciTPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNDLS----- 243

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217283422 207 MLSAHKVIGPEPTGFLLKFNPSLNVVDkIHQNTPLHWAVAAGNVNA-VDKLLEAGSSLDIQNVKGETPLDMALQN 280
Cdd:PHA02876  244 LLKAIRNEDLETSLLLYDAGFSVNSID-DCKNTPLHHASQAPSLSRlVPKLLERGADVNAKNIKGETPLYLMAKN 317
PHA03095 PHA03095
ankyrin-like protein; Provisional
 112-289 8.09e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 80.45  E-value: 8.09e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422 112 NNRLDLVKFYISKGAVVDQLGGdLNSTPLHWAIRQGHLP---MVILLLQHGADPTLIDGEGFSSIHLAVLFQH-MPIIAY 187
Cdd:PHA03095   24 NVTVEEVRRLLAAGADVNFRGE-YGKTPLHLYLHYSSEKvkdIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKL 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422 188 LISKGQSVNMTDVNGQTPlmLSAH---KVIGPEPTGFLLKFNPSLNVVDKiHQNTPLHWAVAAGNVNA--VDKLLEAGSS 262
Cdd:PHA03095  103 LIKAGADVNAKDKVGRTP--LHVYlsgFNINPKVIRLLLRKGADVNALDL-YGMTPLAVLLKSRNANVelLRLLIDAGAD 179

                         170       180
                  ....*....|....*....|....*....
gi 2217283422 263 LDIQNVKGETPLDMALQN--KNQLIIHML 289
Cdd:PHA03095  180 VYAVDDRFRSLLHHHLQSfkPRARIVREL 208
PHA03095 PHA03095
ankyrin-like protein; Provisional
 88-282 1.36e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 79.68  E-value: 1.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422  88 LVEAGYDVRQPDKENVSLLHWAAIN-NRLDLVKFYISKGAVVDQlGGDLNSTPLH------WAirqgHLPMVILLLQHGA 160
Cdd:PHA03095   69 LLEAGADVNAPERCGFTPLHLYLYNaTTLDVIKLLIKAGADVNA-KDKVGRTPLHvylsgfNI----NPKVIRLLLRKGA 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422 161 DPTLIDGEGFSSIHLAVLFQHMPI--IAYLISKGQSVNMTDVNGQTPL---MLSAHK---------VIGPEPTG------ 220
Cdd:PHA03095  144 DVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADVYAVDDRFRSLLhhhLQSFKPrarivreliRAGCDPAAtdmlgn 223

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422 221 ------------------FLLKFNPSLNVVDKIHQnTPLHWAVAAGNVNAVDKLLEAGSSLDIQNVKGETPLDMALQNKN 282
Cdd:PHA03095  224 tplhsmatgssckrslvlPLLIAGISINARNRYGQ-TPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNN 302
Ank_2 pfam12796
Ankyrin repeats (3 copies);
140-267 2.63e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 71.69  E-value: 2.63e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422 140 LHWAIRQGHLPMVILLLQHGADPTLIDGEGFSSIHLAVLFQHMPIIAYLISKGQsVNMTDvngqtplmlsahkvigpept 219
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD-VNLKD-------------------- 59

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2217283422 220 gfllkfnpslnvvdkiHQNTPLHWAVAAGNVNAVDKLLEAGSSLDIQN 267
Cdd:pfam12796  60 ----------------NGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 116-278 1.05e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 70.68  E-value: 1.05e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422 116 DLVKFYISKGAVVDQLGGDLNSTPLHWAIRQGHLPMVILLLQHGADPTLIDGEGFSSIHLAVLFQHMPIIAYLISKGQSV 195
Cdd:PHA02878  148 EITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAST 227

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422 196 NMTDVNGQTPLMLSAHKVIGPEPTGFLLKFNPSLNVVDKIHQNTPLHWAVAAGNVnaVDKLLEAGSSLDIQNVKGETPLD 275
Cdd:PHA02878  228 DARDKCGNTPLHISVGYCKDYDILKLLLEHGVDVNAKSYILGLTALHSSIKSERK--LKLLLEYGADINSLNSYKLTPLS 305


                  ...
gi 2217283422 276 MAL 278
Cdd:PHA02878  306 SAV 308
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 86-245 4.48e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 68.75  E-value: 4.48e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422  86 KELVEAGYDVRQPDKENV-SLLHWAAINNRLDLVKFYISKGAVVDQLgGDLNSTPLHWAIRQGHLPMVILLLQHGADPTL 164
Cdd:PHA02878  151 KLLLSYGADINMKDRHKGnTALHYATENKDQRLTELLLSYGANVNIP-DKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422 165 IDGEGFSSIHLAVLF-QHMPIIAYLISKGQSVNM-TDVNGQTPLMLSAHKvigPEPTGFLLKFNPSLNVVDkIHQNTPLH 242
Cdd:PHA02878  230 RDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAkSYILGLTALHSSIKS---ERKLKLLLEYGADINSLN-SYKLTPLS 305


                  ...
gi 2217283422 243 WAV 245
Cdd:PHA02878  306 SAV 308
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 76-289 5.05e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 65.86  E-value: 5.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422  76 ATQYGIFERCKELVEAGYDVRQPDKENVSLLHWAAINNRLDLVKFYISKGAVVDQlggdlNSTPLHWAIRQGHLPMVILL 155
Cdd:PHA02876  185 AAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINK-----NDLSLLKAIRNEDLETSLLL 259

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422 156 LQHGADPTLIDGEGFSSIHLAVLFQHMP-IIAYLISKGQSVNMTDVNGQTPLMLSAHKVIGPEPTGFLLKFNPSLNVVDK 234
Cdd:PHA02876  260 YDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGYDTENIRTLIMLGADVNAADR 339

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217283422 235 IHqNTPLHWAVAAG-NVNAVDKLLEAGSSLDIQNVKGETPLDMALQNKNQLIIHML 289
Cdd:PHA02876  340 LY-ITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTL 394
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 136-282 1.35e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 63.92  E-value: 1.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422 136 NSTPLHWAIRQGHLPMVILLLQHGADPTLIDGEGFSSIHLAVLFQH-----MPIIAYLISKGQSVNMTDVNGQTPLMLSA 210
Cdd:PHA03100   35 PVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITPLLYAI 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422 211 HKVIG-PEPTGFLLKFNPSLNVVDKIHQNtPLHWAVAAG---------------NVNA---VDKLLEAGSSLDIQNVKGE 271
Cdd:PHA03100  115 SKKSNsYSIVEYLLDNGANVNIKNSDGEN-LLHLYLESNkidlkilkllidkgvDINAknrVNYLLSYGVPINIKDVYGF 193

                         170
                  ....*....|.
gi 2217283422 272 TPLDMALQNKN 282
Cdd:PHA03100  194 TPLHYAVYNNN 204
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 94-276 2.77e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 62.70  E-value: 2.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422  94 DVRQPDKEnvSLLHWAAINNRLDLVKFYISKGAVVDQLGGDLNSTPLHWAIRQGHLPMVILLLQHGADPTLIDGEGFSSI 173
Cdd:PHA02875   62 DVKYPDIE--SELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPL 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422 174 HLAVLFQHMPIIAYLISKGQSVNMTDVNGQTPLMLS-AHKVIgpEPTGFLLKFNPSLNVVDKIHQNTPLHWAVAAGNVNA 252
Cdd:PHA02875  140 HLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAmAKGDI--AICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDI 217

                         170       180
                  ....*....|....*....|....*..
gi 2217283422 253 VDKLLEAGSSLDIQ-NVKGE--TPLDM 276
Cdd:PHA02875  218 VRLFIKRGADCNIMfMIEGEecTILDM 244
Ank_4 pfam13637
Ankyrin repeats (many copies);
136-189 2.33e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.43  E-value: 2.33e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2217283422 136 NSTPLHWAIRQGHLPMVILLLQHGADPTLIDGEGFSSIHLAVLFQHMPIIAYLI 189
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 138-289 2.71e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 59.62  E-value: 2.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422 138 TPLHWAIRQGHLPMVILLLQHGADPTLIDGEGFSSIHLAVLFQHMPIIAYLISKGQSVNmtDV---NGQTPLMLsAHKVI 214
Cdd:PHA02875   37 SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAD--DVfykDGMTPLHL-ATILK 113

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217283422 215 GPEPTGFLLKF--NPSLNVVDKIhqnTPLHWAVAAGNVNAVDKLLEAGSSLDIQNVKGETPLDMALQNKNQLIIHML 289
Cdd:PHA02875  114 KLDIMKLLIARgaDPDIPNTDKF---SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKML 187
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 86-199 4.83e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 58.91  E-value: 4.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422  86 KELVEAGYDVRQPDKENVSLLHWAAINNR--LDLVKFYISKGAVVDQ---------LGGDLNS------TPLHWAIRQGH 148
Cdd:PHA03100  125 EYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAknrvnyllsYGVPINIkdvygfTPLHYAVYNNN 204

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2217283422 149 LPMVILLLQHGADPTLIDGEGFSSIHLAVLFQHMPIIAYLISKGQSVNMTD 199
Cdd:PHA03100  205 PEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTII 255
Ank_4 pfam13637
Ankyrin repeats (many copies);
102-156 1.37e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.12  E-value: 1.37e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2217283422 102 NVSLLHWAAINNRLDLVKFYISKGAVVDQLGGDLNsTPLHWAIRQGHLPMVILLL 156
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGE-TALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
222-277 1.86e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.11  E-value: 1.86e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217283422 222 LLKFNPSLNVVDKIHQNTPLHWAVAAGNVNAVDKLLEAGSSLDIQNVKGETPLDMA 277
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
138-176 8.18e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.19  E-value: 8.18e-07
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2217283422 138 TPLHWAIRQGHLPMVILLLQHGADPTLIDGEGFSSIHLA 176
Cdd:pfam13857  18 TPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02798 PHA02798
ankyrin-like protein; Provisional
 69-289 2.94e-06

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 50.22  E-value: 2.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422  69 SNCDI-VKATQYGIFER-----------CKELVEAGYDVRQPDKENVS-----LLHWAAINNRLDLVKFYISKGAVVDQL 131
Cdd:PHA02798   26 KSCNPnEIVNEYSIFQKylqrdspstdiVKLFINLGANVNGLDNEYSTplctiLSNIKDYKHMLDIVKILIENGADINKK 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422 132 GGDLNsTPLHWAIRQGH---LPMVILLLQHGADPTLIDGEGFSSIHLAVLFQH--------------------------- 181
Cdd:PHA02798  106 NSDGE-TPLYCLLSNGYinnLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHhidieiiklllekgvdinthnnkekyd 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422 182 --------------MPIIAYLISKGQSVNMTDVNGQTPLM------LSAHKVIGPEPTGFLLKFnPSLNVVDKIHQNtPL 241
Cdd:PHA02798  185 tlhcyfkynidridADILKLFVDNGFIINKENKSHKKKFMeylnslLYDNKRFKKNILDFIFSY-IDINQVDELGFN-PL 262

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 2217283422 242 HWAVAAGNVNAVDKLLEAGSSLDIQNVKGETPLDMALQNKNQLIIHML 289
Cdd:PHA02798  263 YYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSI 310
Ank_4 pfam13637
Ankyrin repeats (many copies);
237-289 4.42e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.19  E-value: 4.42e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2217283422 237 QNTPLHWAVAAGNVNAVDKLLEAGSSLDIQNVKGETPLDMALQNKNQLIIHML 289
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 138-166 6.11e-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: 6.11e-06
                          10        20        30
                  ....*....|....*....|....*....|
gi 2217283422 138 TPLHWAI-RQGHLPMVILLLQHGADPTLID 166
Cdd:pfam00023   4 TPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 83-263 6.99e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 49.29  E-value: 6.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422  83 ERCKELVEAGYDVRQPDKENVSLLHWAAINNRldlvkfyiSKGAVVD--QLGGDLNS------TPLHWAIRQGHLPMVIL 154
Cdd:PHA02876  322 ENIRTLIMLGADVNAADRLYITPLHQASTLDR--------NKDIVITllELGANVNArdycdkTPIHYAAVRNNVVIINT 393

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422 155 LLQHGADPTLIDGEGFSSIHLAvLFQHMPIIAY--LISKGQSVNMTDVNGQTPLMLSAHKVIGPEPTGFLLKFNPSLNVV 232
Cdd:PHA02876  394 LLDYGADIEALSQKIGTALHFA-LCGTNPYMSVktLIDRGANVNSKNKDLSTPLHYACKKNCKLDVIEMLLDNGADVNAI 472

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2217283422 233 DkIHQNTPLhwAVAAGNVNAVDKLLEAGSSL 263
Cdd:PHA02876  473 N-IQNQYPL--LIALEYHGIVNILLHYGAEL 500
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 138-164 2.25e-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: 2.25e-05
                           10        20
                   ....*....|....*....|....*..
gi 2217283422  138 TPLHWAIRQGHLPMVILLLQHGADPTL 164
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 134-289 2.37e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 47.27  E-value: 2.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422 134 DLNSTPLHWAIRQGHLPMVILLLQHGADPTLIDGEGFSSIHLAVLFQHMPIIAYLISKGQSVNMTDVngqtplmlsahKV 213
Cdd:PHA02874   33 DETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSILPI-----------PC 101

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217283422 214 IGPEPTGFLLKFNPSLNVVDKiHQNTPLHWAVAAGNVNAVDKLLEAGSSLDIQNVKGETPLDMALQNKNQLIIHML 289
Cdd:PHA02874  102 IEKDMIKTILDCGIDVNIKDA-ELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLL 176
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 132-177 2.84e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.20  E-value: 2.84e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2217283422 132 GGDLNS------TPLHWAIRQGHLPMVILLLQHGADPTLIDGEGFSSIHLAV 177
Cdd:PTZ00322  105 GADPNCrdydgrTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAE 156
Ank_5 pfam13857
Ankyrin repeats (many copies);
155-206 3.06e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 3.06e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2217283422 155 LLQHG-ADPTLIDGEGFSSIHLAVLFQHMPIIAYLISKGQSVNMTDVNGQTPL 206
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
Ank_2 pfam12796
Ankyrin repeats (3 copies);
241-289 5.48e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 42.41  E-value: 5.48e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2217283422 241 LHWAVAAGNVNAVDKLLEAGSSLDIQNVKGETPLDMALQNKNQLIIHML 289
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL 49
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 84-161 6.08e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 45.81  E-value: 6.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422  84 RCKELVEAGYDVRQPDKENVSLLHWAAINNRLDLVKFYISKGA---VVDQLGgdlnSTPLHWAIRQGHLPMVILLLQHGA 160
Cdd:PHA03100  174 RVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGAnpnLVNKYG----DTPLHIAILNNNKEIFKLLLNNGP 249


                  .
gi 2217283422 161 D 161
Cdd:PHA03100  250 S 250
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 139-289 1.09e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 45.26  E-value: 1.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422 139 PLHWAIRQGHLPMVILLLQHGADPTLIDGEGFSSIHLAVLFQHMPIIAYLISK-------------GQSVNMTDVNGQTP 205
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSinkcsvfytlvaiKDAFNNRNVEIFKI 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422 206 LMLSAHK-----------------VIGPEPTGFLLKFNPSLNVVDKIHQNTPLHWAVAAGNVNAVDKLLEAGSSLDIQNV 268
Cdd:PHA02878  120 ILTNRYKniqtidlvyidkkskddIIEAEITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDK 199

                         170       180
                  ....*....|....*....|.
gi 2217283422 269 KGETPLDMALQNKNQLIIHML 289
Cdd:PHA02878  200 TNNSPLHHAVKHYNKPIVHIL 220
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 138-162 1.28e-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: 39.55  E-value: 1.28e-04
                          10        20
                  ....*....|....*....|....*
gi 2217283422 138 TPLHWAIRQGHLPMVILLLQHGADP 162
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADI 28
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 65-279 2.82e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 43.90  E-value: 2.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422  65 IEDSSNCDIVKATQYGIFER-CKELVEAGYDVRQPDKENVSLLHWAAINN-RLDLVKFYISKGAVVDQlGGDLNSTPLHW 142
Cdd:PHA02876  269 IDDCKNTPLHHASQAPSLSRlVPKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNA-ADRLYITPLHQ 347

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422 143 A-IRQGHLPMVILLLQHGADPTLIDGEGFSSIHLAVLFQHMPIIAYLISKGQSVNMTDVNGQTPLMLSAHKVIGPEPTGF 221
Cdd:PHA02876  348 AsTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMSVKT 427

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2217283422 222 LLKFNPSLNVVDKiHQNTPLHWAVAAG-NVNAVDKLLEAGSSLDIQNVKGETPLDMALQ 279
Cdd:PHA02876  428 LIDRGANVNSKNK-DLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIALE 485
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 104-288 3.15e-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: 43.85  E-value: 3.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422 104 SLLHWAAINNRLDLVKFYISKGAVVDQLGGDLNSTPLHWAIRQGHLPMVILLLQhgADPTLIDG-------EGFSSIHLA 176
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNEpmtsdlyQGETALHIA 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422 177 VLFQHMPIIAYLISKGQSVnmtdvngqtplmlsahkvIGPEPTGFLLKFNPSlnvvDKIHQNT-PLHWAVAAGNVNAVDK 255
Cdd:cd22192    97 VVNQNLNLVRELIARGADV------------------VSPRATGTFFRPGPK----NLIYYGEhPLSFAACVGNEEIVRL 154

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2217283422 256 LLEAGSSLDIQNVKGETPLDM-ALQNKNQLIIHM 288
Cdd:cd22192   155 LIEHGADIRAQDSLGNTVLHIlVLQPNKTFACQM 188
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 236-267 4.17e-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: 38.04  E-value: 4.17e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2217283422 236 HQNTPLHWAVA-AGNVNAVDKLLEAGSSLDIQN 267
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 154-209 8.79e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.58  E-value: 8.79e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217283422 154 LLLQHGADPTLIDGEGFSSIHLAVLFQHMPIIAYLISKGQSVNMTDVNGQTPLMLS 209
Cdd:PTZ00322  100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA 155
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 236-265 1.20e-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: 36.80  E-value: 1.20e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 2217283422  236 HQNTPLHWAVAAGNVNAVDKLLEAGSSLDI 265
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 68-281 1.34e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 40.57  E-value: 1.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422  68 SSNCDIVKATQYGIFERCKELVeagYDVRQPDKENVSllHWAAINNRLDlvkfyiskgavvdqlggDLNSTPLHWAIRQG 147
Cdd:PHA02859    5 CSEYDYNDFTDYLFYRYCNPLF---YYVEKDDIEGVK--KWIKFVNDCN-----------------DLYETPIFSCLEKD 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422 148 H--LPMVILLLQHGADPT-LIDGEGFSSIHLAVLFQ---HMPIIAYLISKGQSVNMTDVNGQTPL-MLSAHKVIGPEPTG 220
Cdd:PHA02859   63 KvnVEILKFLIENGADVNfKTRDNNLSALHHYLSFNknvEPEILKILIDSGSSITEEDEDGKNLLhMYMCNFNVRINVIK 142

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217283422 221 FLLKFNPSLNVVDKiHQNTPLH-WAVAAGNVNAVDKLLEAGSSLDIQNVKGETPLDMALQNK 281
Cdd:PHA02859  143 LLIDSGVSFLNKDF-DNNNILYsYILFHSDKKIFDFLTSLGIDINETNKSGYNCYDLIKFRN 203
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 138-285 1.87e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.39  E-value: 1.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422 138 TPLHWAIRQGHLPMVILLLQHGADPTLIDGEGFSSIHLAVLFQHMPIIAYLIskgQSVNMTDVNGQTPLMLSAHKVIGPE 217
Cdd:PLN03192  560 TPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY---HFASISDPHAAGDLLCTAAKRNDLT 636

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217283422 218 PTGFLLKFnpSLNVVDKIHQN-TPLHWAVAAGNVNAVDKLLEAGSSLDiqnvKGETPLDMALQNKNQLI 285
Cdd:PLN03192  637 AMKELLKQ--GLNVDSEDHQGaTALQVAMAEDHVDMVRLLIMNGADVD----KANTDDDFSPTELRELL 699
Ank_4 pfam13637
Ankyrin repeats (many copies);
171-212 2.62e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.48  E-value: 2.62e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2217283422 171 SSIHLAVLFQHMPIIAYLISKGQSVNMTDVNGQTPLMLSAHK 212
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASN 44
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 236-289 3.26e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 40.65  E-value: 3.26e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2217283422 236 HQNTPLHWAVAAGNVNAVDKLLEAGSSLDIQNVKGETPLDMALQNKNQLIIHML 289
Cdd:PTZ00322  114 DGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
PHA03095 PHA03095
ankyrin-like protein; Provisional
 86-191 3.96e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 40.01  E-value: 3.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422  86 KELVEAGYDVRQPDKENVSLLHWAAINN--RLDLVKFYISKGAVVDQLgGDLNSTPLHWAIRQGHLPMVILLLQHGADPT 163
Cdd:PHA03095  206 RELIRAGCDPAATDMLGNTPLHSMATGSscKRSLVLPLLIAGISINAR-NRYGQTPLHYAAVFNNPRACRRLIALGADIN 284

                          90       100
                  ....*....|....*....|....*...
gi 2217283422 164 LIDGEGFSSIHLAVLFQHMPIIAYLISK 191
Cdd:PHA03095  285 AVSSDGNTPLSLMVRNNNGRAVRAALAK 312
PHA02946 PHA02946
ankyin-like protein; Provisional
 50-291 9.89e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 38.88  E-value: 9.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422  50 HENKELANAREALPLIEDSSNCDIVKA--TQYGIFER-CKELVEAGYDVRQPDKENVSLLHWAAINNRLDLVKFYISKGA 126
Cdd:PHA02946   17 YNSKNLDVFRNMLQAIEPSGNYHILHAycGIKGLDERfVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGA 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422 127 vvDQLGGDL-NSTPLHW--AIRQGHLPMVILLLQHGAD-PTLIDGEGFSSIhLAVLFQHMPIIAYLISKGQSVNMTDVNG 202
Cdd:PHA02946   97 --DPNACDKqHKTPLYYlsGTDDEVIERINLLVQYGAKiNNSVDEEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFG 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217283422 203 QTPLmlsaHK-VIGPEPTG----FLLKFNPSLNVVDKiHQNTPLHWAVA--AGNVNAVDKLLEAgSSLDIQNVKGETPLD 275
Cdd:PHA02946  174 KNHI----HRhLMSDNPKAstisWMMKLGISPSKPDH-DGNTPLHIVCSktVKNVDIINLLLPS-TDVNKQNKFGDSPLT 247

                         250
                  ....*....|....*...
gi 2217283422 276 MALQNKN--QLIIHMLKT 291
Cdd:PHA02946  248 LLIKTLSpaHLINKLLST 265
 
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.
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