NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|47933346|ref|NP_061901|]
View 

palmitoyltransferase ZDHHC13 isoform 1 [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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
29-270 1.76e-39

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 146.64  E-value: 1.76e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346  29 AHENKELANAREALPLIEDSSNCDIVKATQYGIFERCKELVEAGYDVRQPDKENVSLLHWAAINNRLDLVKFYISKGAVV 108
Cdd:COG0666   1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346 109 DQLGGDLNsTPLHWAIRQGHLPMVILLLQHGADPTLIDGEGFSSIHLAVLFQHMPIIAYLISKGQSVNMTDVNGQTPLML 188
Cdd:COG0666  81 NAKDDGGN-TLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346 189 SAHKviG-PEPTGFLLKFNPSLNVVDKiHQNTPLHWAVAAGNVNAVDKLLEAGSSLDIQNVKGETPLDMALQNKNQLIIH 267
Cdd:COG0666 160 AAAN--GnLEIVKLLLEAGADVNARDN-DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVK 236


                ...
gi 47933346 268 MLK 270
Cdd:COG0666 237 LLL 239
DHHC pfam01529
DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which ...
 423-559 4.42e-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: 4.42e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346   423 DFRTFCTSCLIRKPLRSLHCHVCNCCVARYDQHCLWTGRCIGFGNHHYYIFFLFFLSMVCGWIIYGSFIYLSSHCATTFK 502
Cdd:pfam01529   3 DELKYCSTCNIYKPPRSKHCRVCNRCVLRFDHHCPWLNNCIGKRNHKYFILFLLYLTLYLILYLVLSLYYLVKLIESSTL 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 47933346   503 EDGLWTYLNQivacspWVLYILMLATFHFSWSTFLLLNQLFQIaFLGLTSHERISLQ 559
Cdd:pfam01529  83 FFFLILFLFS------ISIILLILSLFFLLFLGILLFFHLYLI-SRNLTTYEFMKKK 132
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
29-270 1.76e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 146.64  E-value: 1.76e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346  29 AHENKELANAREALPLIEDSSNCDIVKATQYGIFERCKELVEAGYDVRQPDKENVSLLHWAAINNRLDLVKFYISKGAVV 108
Cdd:COG0666   1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346 109 DQLGGDLNsTPLHWAIRQGHLPMVILLLQHGADPTLIDGEGFSSIHLAVLFQHMPIIAYLISKGQSVNMTDVNGQTPLML 188
Cdd:COG0666  81 NAKDDGGN-TLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346 189 SAHKviG-PEPTGFLLKFNPSLNVVDKiHQNTPLHWAVAAGNVNAVDKLLEAGSSLDIQNVKGETPLDMALQNKNQLIIH 267
Cdd:COG0666 160 AAAN--GnLEIVKLLLEAGADVNARDN-DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVK 236


                ...
gi 47933346 268 MLK 270
Cdd:COG0666 237 LLL 239
DHHC pfam01529
DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which ...
 423-559 4.42e-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: 4.42e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346   423 DFRTFCTSCLIRKPLRSLHCHVCNCCVARYDQHCLWTGRCIGFGNHHYYIFFLFFLSMVCGWIIYGSFIYLSSHCATTFK 502
Cdd:pfam01529   3 DELKYCSTCNIYKPPRSKHCRVCNRCVLRFDHHCPWLNNCIGKRNHKYFILFLLYLTLYLILYLVLSLYYLVKLIESSTL 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 47933346   503 EDGLWTYLNQivacspWVLYILMLATFHFSWSTFLLLNQLFQIaFLGLTSHERISLQ 559
Cdd:pfam01529  83 FFFLILFLFS------ISIILLILSLFFLLFLGILLFFHLYLI-SRNLTTYEFMKKK 132
COG5273 COG5273
Uncharacterized protein containing DHHC-type Zn finger [General function prediction only];
341-588 3.27e-26

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


Pssm-ID: 227598 [Multi-domain]  Cd Length: 309  Bit Score: 109.46  E-value: 3.27e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346 341 YKNLVYLPTAFLLSSVFWIFMTwFILFFPDLAGAPFYFSFIFSIVAFLYFFYKTwaTDPGFTKASEEEKKVN--IITLAE 418
Cdd:COG5273  26 YAYKMFIGLFLLSRIVVYTLLV-IVKSLSLVVLFIILFIVILVLASFSYLLLLV--SDPGYLGENITLSGYRetISRLLD 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346 419 TGSLDFRTFCTSCLIRKPLRSLHCHVCNCCVARYDQHCLWTGRCIGFGNHHYYIFFLFFLSMVcgwIIYgSFIYLSSHCA 498
Cdd:COG5273 103 DGKFGTENFCSTCNIYKPPRSHHCSICNRCVLKFDHHCPWINNCVGFRNYRFFYQFLLYTILV---ALV-VLLSTAYYIA 178

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346 499 TTFKEDGLWTYLNQIVACSPWVLYILMLATFHFSW--STFLLLNQLFQIAFL-----GLTSHERISLQKQSKHMKQTLSL 571
Cdd:COG5273 179 GIFSIRHDTSLAICFLIFGCSLLGVVFFIITTLLLlfLIYLILNNLTTIEFIqisrgGSTLEFFPLCRESNLPFTNIFDS 258

                       250
                ....*....|....*....
gi 47933346 572 RKT--PYNLGFMQNLADFF 588
Cdd:COG5273 259 SEGalPLDLGIGQNLSTIK 277
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 66-269 2.23e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 90.88  E-value: 2.23e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346   66 KELVEAGYDVRQPDKENVSLLHWAA-----INNRLDLVKFYISKGAVVDQlGGDLNSTPLHWAI--RQGHLPMVILLLQH 138
Cdd:PHA03100  52 KILLDNGADINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLEYGANVNA-PDNNGITPLLYAIskKSNSYSIVEYLLDN 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346  139 GADPTLIDGEGFSSIHLAVLFQH--MPIIAYLISKGQSVN-MTDVNgqtplmlsahkvigpeptgFLLKFNPSLNVVDKI 215
Cdd:PHA03100 131 GANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINaKNRVN-------------------YLLSYGVPINIKDVY 191

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 47933346  216 HqNTPLHWAVAAGNVNAVDKLLEAGSSLDIQNVKGETPLDMALQNKNQLIIHML 269
Cdd:PHA03100 192 G-FTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLL 244
Ank_2 pfam12796
Ankyrin repeats (3 copies);
56-146 1.32e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.93  E-value: 1.32e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346    56 ATQYGIFERCKELVEAGYDVRQPDKENVSLLHWAAINNRLDLVKFYISKGAVVDQLGGDlnsTPLHWAIRQGHLPMVILL 135
Cdd:pfam12796   4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR---TALHYAARSGHLEIVKLL 80

                          90
                  ....*....|.
gi 47933346   136 LQHGADPTLID 146
Cdd:pfam12796  81 LEKGADINVKD 91
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 118-144 2.74e-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: 2.74e-05
                           10        20
                   ....*....|....*....|....*..
gi 47933346    118 TPLHWAIRQGHLPMVILLLQHGADPTL 144
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 84-268 3.40e-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: 43.46  E-value: 3.40e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346  84 SLLHWAAINNRLDLVKFYISKGAVVDQLGGDLNSTPLHWAIRQGHLPMVILLLQhgADPTLIDG-------EGFSSIHLA 156
Cdd:cd22192  19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNEpmtsdlyQGETALHIA 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346 157 VLFQHMPIIAYLISKGQSVnmtdvngqtplmlsahkvIGPEPTGFLLKFNPSlnvvDKIHQNT-PLHWAVAAGNVNAVDK 235
Cdd:cd22192  97 VVNQNLNLVRELIARGADV------------------VSPRATGTFFRPGPK----NLIYYGEhPLSFAACVGNEEIVRL 154

                       170       180       190
                ....*....|....*....|....*....|....
gi 47933346 236 LLEAGSSLDIQNVKGETPLDM-ALQNKNQLIIHM 268
Cdd:cd22192 155 LIEHGADIRAQDSLGNTVLHIlVLQPNKTFACQM 188
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
29-270 1.76e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 146.64  E-value: 1.76e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346  29 AHENKELANAREALPLIEDSSNCDIVKATQYGIFERCKELVEAGYDVRQPDKENVSLLHWAAINNRLDLVKFYISKGAVV 108
Cdd:COG0666   1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346 109 DQLGGDLNsTPLHWAIRQGHLPMVILLLQHGADPTLIDGEGFSSIHLAVLFQHMPIIAYLISKGQSVNMTDVNGQTPLML 188
Cdd:COG0666  81 NAKDDGGN-TLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346 189 SAHKviG-PEPTGFLLKFNPSLNVVDKiHQNTPLHWAVAAGNVNAVDKLLEAGSSLDIQNVKGETPLDMALQNKNQLIIH 267
Cdd:COG0666 160 AAAN--GnLEIVKLLLEAGADVNARDN-DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVK 236


                ...
gi 47933346 268 MLK 270
Cdd:COG0666 237 LLL 239
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
29-280 2.45e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 146.25  E-value: 2.45e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346  29 AHENKELANAREALPLIEDSSNCDIVKATQYGIFERCKELVEAGYDVRQPDKENVSLLHWAAINNRLDLVKFYISKGAVV 108
Cdd:COG0666  34 LLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADV 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346 109 DQLGGDLNsTPLHWAIRQGHLPMVILLLQHGADPTLIDGEGFSSIHLAVLFQHMPIIAYLISKGQSVNMTDVNGQTPLML 188
Cdd:COG0666 114 NARDKDGE-TPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHL 192

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346 189 SAHKviG-PEPTGFLLKFNPSLNVVDKiHQNTPLHWAVAAGNVNAVDKLLEAGSSLDIQNVKGETPLDMALQNKNQLIIH 267
Cdd:COG0666 193 AAEN--GhLEIVKLLLEAGADVNAKDN-DGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVK 269

                       250
                ....*....|...
gi 47933346 268 MLKTEAKMRANQK 280
Cdd:COG0666 270 LLLLALLLLAAAL 282
DHHC pfam01529
DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which ...
 423-559 4.42e-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: 4.42e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346   423 DFRTFCTSCLIRKPLRSLHCHVCNCCVARYDQHCLWTGRCIGFGNHHYYIFFLFFLSMVCGWIIYGSFIYLSSHCATTFK 502
Cdd:pfam01529   3 DELKYCSTCNIYKPPRSKHCRVCNRCVLRFDHHCPWLNNCIGKRNHKYFILFLLYLTLYLILYLVLSLYYLVKLIESSTL 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 47933346   503 EDGLWTYLNQivacspWVLYILMLATFHFSWSTFLLLNQLFQIaFLGLTSHERISLQ 559
Cdd:pfam01529  83 FFFLILFLFS------ISIILLILSLFFLLFLGILLFFHLYLI-SRNLTTYEFMKKK 132
COG5273 COG5273
Uncharacterized protein containing DHHC-type Zn finger [General function prediction only];
341-588 3.27e-26

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


Pssm-ID: 227598 [Multi-domain]  Cd Length: 309  Bit Score: 109.46  E-value: 3.27e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346 341 YKNLVYLPTAFLLSSVFWIFMTwFILFFPDLAGAPFYFSFIFSIVAFLYFFYKTwaTDPGFTKASEEEKKVN--IITLAE 418
Cdd:COG5273  26 YAYKMFIGLFLLSRIVVYTLLV-IVKSLSLVVLFIILFIVILVLASFSYLLLLV--SDPGYLGENITLSGYRetISRLLD 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346 419 TGSLDFRTFCTSCLIRKPLRSLHCHVCNCCVARYDQHCLWTGRCIGFGNHHYYIFFLFFLSMVcgwIIYgSFIYLSSHCA 498
Cdd:COG5273 103 DGKFGTENFCSTCNIYKPPRSHHCSICNRCVLKFDHHCPWINNCVGFRNYRFFYQFLLYTILV---ALV-VLLSTAYYIA 178

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346 499 TTFKEDGLWTYLNQIVACSPWVLYILMLATFHFSW--STFLLLNQLFQIAFL-----GLTSHERISLQKQSKHMKQTLSL 571
Cdd:COG5273 179 GIFSIRHDTSLAICFLIFGCSLLGVVFFIITTLLLlfLIYLILNNLTTIEFIqisrgGSTLEFFPLCRESNLPFTNIFDS 258

                       250
                ....*....|....*....
gi 47933346 572 RKT--PYNLGFMQNLADFF 588
Cdd:COG5273 259 SEGalPLDLGIGQNLSTIK 277
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 66-269 2.23e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 90.88  E-value: 2.23e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346   66 KELVEAGYDVRQPDKENVSLLHWAA-----INNRLDLVKFYISKGAVVDQlGGDLNSTPLHWAI--RQGHLPMVILLLQH 138
Cdd:PHA03100  52 KILLDNGADINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLEYGANVNA-PDNNGITPLLYAIskKSNSYSIVEYLLDN 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346  139 GADPTLIDGEGFSSIHLAVLFQH--MPIIAYLISKGQSVN-MTDVNgqtplmlsahkvigpeptgFLLKFNPSLNVVDKI 215
Cdd:PHA03100 131 GANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINaKNRVN-------------------YLLSYGVPINIKDVY 191

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 47933346  216 HqNTPLHWAVAAGNVNAVDKLLEAGSSLDIQNVKGETPLDMALQNKNQLIIHML 269
Cdd:PHA03100 192 G-FTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLL 244
Ank_2 pfam12796
Ankyrin repeats (3 copies);
56-146 1.32e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.93  E-value: 1.32e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346    56 ATQYGIFERCKELVEAGYDVRQPDKENVSLLHWAAINNRLDLVKFYISKGAVVDQLGGDlnsTPLHWAIRQGHLPMVILL 135
Cdd:pfam12796   4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR---TALHYAARSGHLEIVKLL 80

                          90
                  ....*....|.
gi 47933346   136 LQHGADPTLID 146
Cdd:pfam12796  81 LEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
86-179 2.83e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.08  E-value: 2.83e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346    86 LHWAAINNRLDLVKFYISKGAVVDQLGGDlNSTPLHWAIRQGHLPMVILLLQHGAdpTLIDGEGFSSIHLAVLFQHMPII 165
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKN-GRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIV 77

                          90
                  ....*....|....
gi 47933346   166 AYLISKGQSVNMTD 179
Cdd:pfam12796  78 KLLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 63-264 6.75e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 83.47  E-value: 6.75e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346   63 ERCKELVEAGYDVRQPDKENVSLLHWAAINNRLDLVKFYISKGAVVDqLGGDLNSTPLHWAIRQGHLPMVILLLQHGADP 142
Cdd:PHA02874 105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVN-IEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYA 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346  143 TLIDGEGFSSIHLAVLFQHMPIIAYLISKGQSVNMTDVNGQTPLmlsaHKVIGPEPTGF-LLKFNPSLNVVDkIHQNTPL 221
Cdd:PHA02874 184 NVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPL----HNAIIHNRSAIeLLINNASINDQD-IDGSTPL 258

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 47933346  222 HWAVA-AGNVNAVDKLLEAGSSLDIQNVKGETPLDMALQNKNQL 264
Cdd:PHA02874 259 HHAINpPCDIDIIDILLYHKADISIKDNKGENPIDTAFKYINKD 302
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
56-186 9.15e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 81.15  E-value: 9.15e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346  56 ATQYGIFERCKELVEAGYDVRQPDKENVSLLHWAAINNRLDLVKFYISKGAVVDQLGGDLNsTPLHWAIRQGHLPMVILL 135
Cdd:COG0666 160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGK-TALDLAAENGNLEIVKLL 238

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 47933346 136 LQHGADPTLIDGEGFSSIHLAVLFQHMPIIAYLISKGQSVNMTDVNGQTPL 186
Cdd:COG0666 239 LEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 44-260 2.11e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 82.80  E-value: 2.11e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346   44 LIEDSSNCDIVKATQYG--------IFERCKELVE---AGYDVRQpDKENVSLLHWAAINNRLDLVKFYISKgaVVDQLG 112
Cdd:PHA02876  92 VISLTLDCDIILDIKYAsiilnkhkLDEACIHILKeaiSGNDIHY-DKINESIEYMKLIKERIQQDELLIAE--MLLEGG 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346  113 GDLNS------TPLHWAIRQGHLPMVILLLQHGADPTLIDGEGFSSIHLAVLFQHMPIIAYLISKGQSVNMTDVNgqtpl 186
Cdd:PHA02876 169 ADVNAkdiyciTPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNDLS----- 243

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47933346  187 MLSAHKVIGPEPTGFLLKFNPSLNVVDkIHQNTPLHWAVAAGNVNA-VDKLLEAGSSLDIQNVKGETPLDMALQN 260
Cdd:PHA02876 244 LLKAIRNEDLETSLLLYDAGFSVNSID-DCKNTPLHHASQAPSLSRlVPKLLERGADVNAKNIKGETPLYLMAKN 317
PHA03095 PHA03095
ankyrin-like protein; Provisional
 92-269 8.48e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 80.07  E-value: 8.48e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346   92 NNRLDLVKFYISKGAVVDQLGGdLNSTPLHWAIRQGHLP---MVILLLQHGADPTLIDGEGFSSIHLAVLFQH-MPIIAY 167
Cdd:PHA03095  24 NVTVEEVRRLLAAGADVNFRGE-YGKTPLHLYLHYSSEKvkdIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKL 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346  168 LISKGQSVNMTDVNGQTPlmLSAH---KVIGPEPTGFLLKFNPSLNVVDKiHQNTPLHWAVAAGNVNA--VDKLLEAGSS 242
Cdd:PHA03095 103 LIKAGADVNAKDKVGRTP--LHVYlsgFNINPKVIRLLLRKGADVNALDL-YGMTPLAVLLKSRNANVelLRLLIDAGAD 179

                        170       180
                 ....*....|....*....|....*....
gi 47933346  243 LDIQNVKGETPLDMALQN--KNQLIIHML 269
Cdd:PHA03095 180 VYAVDDRFRSLLHHHLQSfkPRARIVREL 208
PHA03095 PHA03095
ankyrin-like protein; Provisional
 68-262 1.46e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 79.68  E-value: 1.46e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346   68 LVEAGYDVRQPDKENVSLLHWAAIN-NRLDLVKFYISKGAVVDQlGGDLNSTPLH------WAirqgHLPMVILLLQHGA 140
Cdd:PHA03095  69 LLEAGADVNAPERCGFTPLHLYLYNaTTLDVIKLLIKAGADVNA-KDKVGRTPLHvylsgfNI----NPKVIRLLLRKGA 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346  141 DPTLIDGEGFSSIHLAVLFQHMPI--IAYLISKGQSVNMTDVNGQTPL---MLSAHK---------VIGPEPTG------ 200
Cdd:PHA03095 144 DVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADVYAVDDRFRSLLhhhLQSFKPrarivreliRAGCDPAAtdmlgn 223

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346  201 ------------------FLLKFNPSLNVVDKIHQnTPLHWAVAAGNVNAVDKLLEAGSSLDIQNVKGETPLDMALQNKN 262
Cdd:PHA03095 224 tplhsmatgssckrslvlPLLIAGISINARNRYGQ-TPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNN 302
Ank_2 pfam12796
Ankyrin repeats (3 copies);
120-247 4.43e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.92  E-value: 4.43e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346   120 LHWAIRQGHLPMVILLLQHGADPTLIDGEGFSSIHLAVLFQHMPIIAYLISKGQsVNMTDvngqtplmlsahkvigpept 199
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD-VNLKD-------------------- 59

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 47933346   200 gfllkfnpslnvvdkiHQNTPLHWAVAAGNVNAVDKLLEAGSSLDIQN 247
Cdd:pfam12796  60 ----------------NGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 96-258 9.88e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 70.68  E-value: 9.88e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346   96 DLVKFYISKGAVVDQLGGDLNSTPLHWAIRQGHLPMVILLLQHGADPTLIDGEGFSSIHLAVLFQHMPIIAYLISKGQSV 175
Cdd:PHA02878 148 EITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAST 227

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346  176 NMTDVNGQTPLMLSAHKVIGPEPTGFLLKFNPSLNVVDKIHQNTPLHWAVAAGNVnaVDKLLEAGSSLDIQNVKGETPLD 255
Cdd:PHA02878 228 DARDKCGNTPLHISVGYCKDYDILKLLLEHGVDVNAKSYILGLTALHSSIKSERK--LKLLLEYGADINSLNSYKLTPLS 305


                 ...
gi 47933346  256 MAL 258
Cdd:PHA02878 306 SAV 308
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 66-225 4.17e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 68.75  E-value: 4.17e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346   66 KELVEAGYDVRQPDKENV-SLLHWAAINNRLDLVKFYISKGAVVDQLgGDLNSTPLHWAIRQGHLPMVILLLQHGADPTL 144
Cdd:PHA02878 151 KLLLSYGADINMKDRHKGnTALHYATENKDQRLTELLLSYGANVNIP-DKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346  145 IDGEGFSSIHLAVLF-QHMPIIAYLISKGQSVNM-TDVNGQTPLMLSAHKvigPEPTGFLLKFNPSLNVVDkIHQNTPLH 222
Cdd:PHA02878 230 RDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAkSYILGLTALHSSIKS---ERKLKLLLEYGADINSLN-SYKLTPLS 305


                 ...
gi 47933346  223 WAV 225
Cdd:PHA02878 306 SAV 308
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 56-269 4.79e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 65.86  E-value: 4.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346   56 ATQYGIFERCKELVEAGYDVRQPDKENVSLLHWAAINNRLDLVKFYISKGAVVDQlggdlNSTPLHWAIRQGHLPMVILL 135
Cdd:PHA02876 185 AAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINK-----NDLSLLKAIRNEDLETSLLL 259

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346  136 LQHGADPTLIDGEGFSSIHLAVLFQHMP-IIAYLISKGQSVNMTDVNGQTPLMLSAHKVIGPEPTGFLLKFNPSLNVVDK 214
Cdd:PHA02876 260 YDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGYDTENIRTLIMLGADVNAADR 339

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 47933346  215 IHqNTPLHWAVAAG-NVNAVDKLLEAGSSLDIQNVKGETPLDMALQNKNQLIIHML 269
Cdd:PHA02876 340 LY-ITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTL 394
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 116-262 1.21e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 63.92  E-value: 1.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346  116 NSTPLHWAIRQGHLPMVILLLQHGADPTLIDGEGFSSIHLAVLFQH-----MPIIAYLISKGQSVNMTDVNGQTPLMLSA 190
Cdd:PHA03100  35 PVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITPLLYAI 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346  191 HKVIG-PEPTGFLLKFNPSLNVVDKIHQNtPLHWAVAAG---------------NVNA---VDKLLEAGSSLDIQNVKGE 251
Cdd:PHA03100 115 SKKSNsYSIVEYLLDNGANVNIKNSDGEN-LLHLYLESNkidlkilkllidkgvDINAknrVNYLLSYGVPINIKDVYGF 193

                        170
                 ....*....|.
gi 47933346  252 TPLDMALQNKN 262
Cdd:PHA03100 194 TPLHYAVYNNN 204
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 74-256 2.64e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 62.70  E-value: 2.64e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346   74 DVRQPDKEnvSLLHWAAINNRLDLVKFYISKGAVVDQLGGDLNSTPLHWAIRQGHLPMVILLLQHGADPTLIDGEGFSSI 153
Cdd:PHA02875  62 DVKYPDIE--SELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPL 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346  154 HLAVLFQHMPIIAYLISKGQSVNMTDVNGQTPLMLS-AHKVIgpEPTGFLLKFNPSLNVVDKIHQNTPLHWAVAAGNVNA 232
Cdd:PHA02875 140 HLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAmAKGDI--AICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDI 217

                        170       180
                 ....*....|....*....|....*..
gi 47933346  233 VDKLLEAGSSLDIQ-NVKGE--TPLDM 256
Cdd:PHA02875 218 VRLFIKRGADCNIMfMIEGEecTILDM 244
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 118-269 2.59e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 59.62  E-value: 2.59e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346  118 TPLHWAIRQGHLPMVILLLQHGADPTLIDGEGFSSIHLAVLFQHMPIIAYLISKGQSVNmtDV---NGQTPLMLsAHKVI 194
Cdd:PHA02875  37 SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAD--DVfykDGMTPLHL-ATILK 113

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47933346  195 GPEPTGFLLKF--NPSLNVVDKIhqnTPLHWAVAAGNVNAVDKLLEAGSSLDIQNVKGETPLDMALQNKNQLIIHML 269
Cdd:PHA02875 114 KLDIMKLLIARgaDPDIPNTDKF---SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKML 187
Ank_4 pfam13637
Ankyrin repeats (many copies);
116-169 3.12e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.05  E-value: 3.12e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 47933346   116 NSTPLHWAIRQGHLPMVILLLQHGADPTLIDGEGFSSIHLAVLFQHMPIIAYLI 169
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 66-179 4.29e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 58.91  E-value: 4.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346   66 KELVEAGYDVRQPDKENVSLLHWAAINNR--LDLVKFYISKGAVVDQ---------LGGDLNS------TPLHWAIRQGH 128
Cdd:PHA03100 125 EYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAknrvnyllsYGVPINIkdvygfTPLHYAVYNNN 204

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 47933346  129 LPMVILLLQHGADPTLIDGEGFSSIHLAVLFQHMPIIAYLISKGQSVNMTD 179
Cdd:PHA03100 205 PEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTII 255
Ank_4 pfam13637
Ankyrin repeats (many copies);
82-136 1.95e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.74  E-value: 1.95e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 47933346    82 NVSLLHWAAINNRLDLVKFYISKGAVVDQLGGDLNsTPLHWAIRQGHLPMVILLL 136
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGE-TALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
202-257 2.24e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.73  E-value: 2.24e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 47933346   202 LLKFNPSLNVVDKIHQNTPLHWAVAAGNVNAVDKLLEAGSSLDIQNVKGETPLDMA 257
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
118-156 9.93e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.19  E-value: 9.93e-07
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 47933346   118 TPLHWAIRQGHLPMVILLLQHGADPTLIDGEGFSSIHLA 156
Cdd:pfam13857  18 TPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02798 PHA02798
ankyrin-like protein; Provisional
 49-269 2.64e-06

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 50.22  E-value: 2.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346   49 SNCDI-VKATQYGIFER-----------CKELVEAGYDVRQPDKENVS-----LLHWAAINNRLDLVKFYISKGAVVDQL 111
Cdd:PHA02798  26 KSCNPnEIVNEYSIFQKylqrdspstdiVKLFINLGANVNGLDNEYSTplctiLSNIKDYKHMLDIVKILIENGADINKK 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346  112 GGDLNsTPLHWAIRQGH---LPMVILLLQHGADPTLIDGEGFSSIHLAVLFQH--------------------------- 161
Cdd:PHA02798 106 NSDGE-TPLYCLLSNGYinnLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHhidieiiklllekgvdinthnnkekyd 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346  162 --------------MPIIAYLISKGQSVNMTDVNGQTPLM------LSAHKVIGPEPTGFLLKFnPSLNVVDKIHQNtPL 221
Cdd:PHA02798 185 tlhcyfkynidridADILKLFVDNGFIINKENKSHKKKFMeylnslLYDNKRFKKNILDFIFSY-IDINQVDELGFN-PL 262

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 47933346  222 HWAVAAGNVNAVDKLLEAGSSLDIQNVKGETPLDMALQNKNQLIIHML 269
Cdd:PHA02798 263 YYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSI 310
Ank_4 pfam13637
Ankyrin repeats (many copies);
217-269 5.58e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.80  E-value: 5.58e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 47933346   217 QNTPLHWAVAAGNVNAVDKLLEAGSSLDIQNVKGETPLDMALQNKNQLIIHML 269
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 63-243 6.68e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 49.29  E-value: 6.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346   63 ERCKELVEAGYDVRQPDKENVSLLHWAAINNRldlvkfyiSKGAVVD--QLGGDLNS------TPLHWAIRQGHLPMVIL 134
Cdd:PHA02876 322 ENIRTLIMLGADVNAADRLYITPLHQASTLDR--------NKDIVITllELGANVNArdycdkTPIHYAAVRNNVVIINT 393

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346  135 LLQHGADPTLIDGEGFSSIHLAvLFQHMPIIAY--LISKGQSVNMTDVNGQTPLMLSAHKVIGPEPTGFLLKFNPSLNVV 212
Cdd:PHA02876 394 LLDYGADIEALSQKIGTALHFA-LCGTNPYMSVktLIDRGANVNSKNKDLSTPLHYACKKNCKLDVIEMLLDNGADVNAI 472

                        170       180       190
                 ....*....|....*....|....*....|.
gi 47933346  213 DkIHQNTPLhwAVAAGNVNAVDKLLEAGSSL 243
Cdd:PHA02876 473 N-IQNQYPL--LIALEYHGIVNILLHYGAEL 500
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 118-146 7.64e-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: 7.64e-06
                          10        20        30
                  ....*....|....*....|....*....|
gi 47933346   118 TPLHWAI-RQGHLPMVILLLQHGADPTLID 146
Cdd:pfam00023   4 TPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 114-269 2.27e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 47.27  E-value: 2.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346  114 DLNSTPLHWAIRQGHLPMVILLLQHGADPTLIDGEGFSSIHLAVLFQHMPIIAYLISKGQSVNMTDVngqtplmlsahKV 193
Cdd:PHA02874  33 DETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSILPI-----------PC 101

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47933346  194 IGPEPTGFLLKFNPSLNVVDKiHQNTPLHWAVAAGNVNAVDKLLEAGSSLDIQNVKGETPLDMALQNKNQLIIHML 269
Cdd:PHA02874 102 IEKDMIKTILDCGIDVNIKDA-ELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLL 176
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 47933346  112 GGDLNS------TPLHWAIRQGHLPMVILLLQHGADPTLIDGEGFSSIHLAV 157
Cdd:PTZ00322 105 GADPNCrdydgrTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAE 156
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 118-144 2.74e-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: 2.74e-05
                           10        20
                   ....*....|....*....|....*..
gi 47933346    118 TPLHWAIRQGHLPMVILLLQHGADPTL 144
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
135-186 3.83e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.56  E-value: 3.83e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 47933346   135 LLQHG-ADPTLIDGEGFSSIHLAVLFQHMPIIAYLISKGQSVNMTDVNGQTPL 186
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 64-141 5.62e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 45.81  E-value: 5.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346   64 RCKELVEAGYDVRQPDKENVSLLHWAAINNRLDLVKFYISKGA---VVDQLGgdlnSTPLHWAIRQGHLPMVILLLQHGA 140
Cdd:PHA03100 174 RVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGAnpnLVNKYG----DTPLHIAILNNNKEIFKLLLNNGP 249


                 .
gi 47933346  141 D 141
Cdd:PHA03100 250 S 250
Ank_2 pfam12796
Ankyrin repeats (3 copies);
221-269 7.10e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 42.03  E-value: 7.10e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 47933346   221 LHWAVAAGNVNAVDKLLEAGSSLDIQNVKGETPLDMALQNKNQLIIHML 269
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL 49
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 119-269 1.05e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 45.26  E-value: 1.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346  119 PLHWAIRQGHLPMVILLLQHGADPTLIDGEGFSSIHLAVLFQHMPIIAYLISK-------------GQSVNMTDVNGQTP 185
Cdd:PHA02878  40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSinkcsvfytlvaiKDAFNNRNVEIFKI 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346  186 LMLSAHK-----------------VIGPEPTGFLLKFNPSLNVVDKIHQNTPLHWAVAAGNVNAVDKLLEAGSSLDIQNV 248
Cdd:PHA02878 120 ILTNRYKniqtidlvyidkkskddIIEAEITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDK 199

                        170       180
                 ....*....|....*....|.
gi 47933346  249 KGETPLDMALQNKNQLIIHML 269
Cdd:PHA02878 200 TNNSPLHHAVKHYNKPIVHIL 220
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 118-142 1.63e-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: 1.63e-04
                          10        20
                  ....*....|....*....|....*
gi 47933346   118 TPLHWAIRQGHLPMVILLLQHGADP 142
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADI 28
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 45-259 2.71e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 43.90  E-value: 2.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346   45 IEDSSNCDIVKATQYGIFER-CKELVEAGYDVRQPDKENVSLLHWAAINN-RLDLVKFYISKGAVVDQlGGDLNSTPLHW 122
Cdd:PHA02876 269 IDDCKNTPLHHASQAPSLSRlVPKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNA-ADRLYITPLHQ 347

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346  123 A-IRQGHLPMVILLLQHGADPTLIDGEGFSSIHLAVLFQHMPIIAYLISKGQSVNMTDVNGQTPLMLSAHKVIGPEPTGF 201
Cdd:PHA02876 348 AsTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMSVKT 427

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 47933346  202 LLKFNPSLNVVDKiHQNTPLHWAVAAG-NVNAVDKLLEAGSSLDIQNVKGETPLDMALQ 259
Cdd:PHA02876 428 LIDRGANVNSKNK-DLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIALE 485
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 84-268 3.40e-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: 43.46  E-value: 3.40e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346  84 SLLHWAAINNRLDLVKFYISKGAVVDQLGGDLNSTPLHWAIRQGHLPMVILLLQhgADPTLIDG-------EGFSSIHLA 156
Cdd:cd22192  19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNEpmtsdlyQGETALHIA 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346 157 VLFQHMPIIAYLISKGQSVnmtdvngqtplmlsahkvIGPEPTGFLLKFNPSlnvvDKIHQNT-PLHWAVAAGNVNAVDK 235
Cdd:cd22192  97 VVNQNLNLVRELIARGADV------------------VSPRATGTFFRPGPK----NLIYYGEhPLSFAACVGNEEIVRL 154

                       170       180       190
                ....*....|....*....|....*....|....
gi 47933346 236 LLEAGSSLDIQNVKGETPLDM-ALQNKNQLIIHM 268
Cdd:cd22192 155 LIEHGADIRAQDSLGNTVLHIlVLQPNKTFACQM 188
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 216-247 5.11e-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: 37.65  E-value: 5.11e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 47933346   216 HQNTPLHWAVA-AGNVNAVDKLLEAGSSLDIQN 247
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
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 47933346  134 LLLQHGADPTLIDGEGFSSIHLAVLFQHMPIIAYLISKGQSVNMTDVNGQTPLMLS 189
Cdd:PTZ00322 100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA 155
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 48-261 1.22e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 40.57  E-value: 1.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346   48 SSNCDIVKATQYGIFERCKELVeagYDVRQPDKENVSllHWAAINNRLDlvkfyiskgavvdqlggDLNSTPLHWAIRQG 127
Cdd:PHA02859   5 CSEYDYNDFTDYLFYRYCNPLF---YYVEKDDIEGVK--KWIKFVNDCN-----------------DLYETPIFSCLEKD 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346  128 H--LPMVILLLQHGADPT-LIDGEGFSSIHLAVLFQ---HMPIIAYLISKGQSVNMTDVNGQTPL-MLSAHKVIGPEPTG 200
Cdd:PHA02859  63 KvnVEILKFLIENGADVNfKTRDNNLSALHHYLSFNknvEPEILKILIDSGSSITEEDEDGKNLLhMYMCNFNVRINVIK 142

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47933346  201 FLLKFNPSLNVVDKiHQNTPLH-WAVAAGNVNAVDKLLEAGSSLDIQNVKGETPLDMALQNK 261
Cdd:PHA02859 143 LLIDSGVSFLNKDF-DNNNILYsYILFHSDKKIFDFLTSLGIDINETNKSGYNCYDLIKFRN 203
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 216-245 1.44e-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: 36.41  E-value: 1.44e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 47933346    216 HQNTPLHWAVAAGNVNAVDKLLEAGSSLDI 245
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 118-265 1.79e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.39  E-value: 1.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346  118 TPLHWAIRQGHLPMVILLLQHGADPTLIDGEGFSSIHLAVLFQHMPIIAYLIskgQSVNMTDVNGQTPLMLSAHKVIGPE 197
Cdd:PLN03192 560 TPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY---HFASISDPHAAGDLLCTAAKRNDLT 636

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47933346  198 PTGFLLKFnpSLNVVDKIHQN-TPLHWAVAAGNVNAVDKLLEAGSSLDiqnvKGETPLDMALQNKNQLI 265
Cdd:PLN03192 637 AMKELLKQ--GLNVDSEDHQGaTALQVAMAEDHVDMVRLLIMNGADVD----KANTDDDFSPTELRELL 699
Ank_4 pfam13637
Ankyrin repeats (many copies);
151-192 3.12e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.10  E-value: 3.12e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 47933346   151 SSIHLAVLFQHMPIIAYLISKGQSVNMTDVNGQTPLMLSAHK 192
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASN 44
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 216-269 3.13e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 40.65  E-value: 3.13e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 47933346  216 HQNTPLHWAVAAGNVNAVDKLLEAGSSLDIQNVKGETPLDMALQNKNQLIIHML 269
Cdd:PTZ00322 114 DGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
PHA03095 PHA03095
ankyrin-like protein; Provisional
 66-171 3.80e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 40.01  E-value: 3.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346   66 KELVEAGYDVRQPDKENVSLLHWAAINN--RLDLVKFYISKGAVVDQLgGDLNSTPLHWAIRQGHLPMVILLLQHGADPT 143
Cdd:PHA03095 206 RELIRAGCDPAATDMLGNTPLHSMATGSscKRSLVLPLLIAGISINAR-NRYGQTPLHYAAVFNNPRACRRLIALGADIN 284

                         90       100
                 ....*....|....*....|....*...
gi 47933346  144 LIDGEGFSSIHLAVLFQHMPIIAYLISK 171
Cdd:PHA03095 285 AVSSDGNTPLSLMVRNNNGRAVRAALAK 312
PHA02946 PHA02946
ankyin-like protein; Provisional
 30-271 8.72e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 38.88  E-value: 8.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346   30 HENKELANAREALPLIEDSSNCDIVKA--TQYGIFER-CKELVEAGYDVRQPDKENVSLLHWAAINNRLDLVKFYISKGA 106
Cdd:PHA02946  17 YNSKNLDVFRNMLQAIEPSGNYHILHAycGIKGLDERfVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGA 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346  107 vvDQLGGDL-NSTPLHW--AIRQGHLPMVILLLQHGAD-PTLIDGEGFSSIhLAVLFQHMPIIAYLISKGQSVNMTDVNG 182
Cdd:PHA02946  97 --DPNACDKqHKTPLYYlsGTDDEVIERINLLVQYGAKiNNSVDEEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFG 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933346  183 QTPLmlsaHK-VIGPEPTG----FLLKFNPSLNVVDKiHQNTPLHWAVA--AGNVNAVDKLLEAgSSLDIQNVKGETPLD 255
Cdd:PHA02946 174 KNHI----HRhLMSDNPKAstisWMMKLGISPSKPDH-DGNTPLHIVCSktVKNVDIINLLLPS-TDVNKQNKFGDSPLT 247

                        250
                 ....*....|....*...
gi 47933346  256 MALQNKN--QLIIHMLKT 271
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.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH