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Conserved domains on  [gi|79517230|ref|NP_197535|]
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Ankyrin repeat family protein with DHHC zinc finger domain-containing protein [Arabidopsis thaliana]

Protein Classification

ankyrin repeat domain-containing DHHC palmitoyltransferase family protein( domain architecture ID 12789670)

ankyrin (ANK) repeat domain-containing DHHC palmitoyltransferase family protein, similar to palmitoyltransferase AKR1 is a palmitoyltransferase specific for casein kinase 1

EC:  2.3.1.225
Gene Ontology:  GO:0016409|GO:0005515
PubMed:  17176038|16582420

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
33-264 2.77e-40

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 148.56  E-value: 2.77e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230  33 NDVYTAAAYGDLEKLHRLVECEGSSVSEPDALGYYALQWSALNNRVAVAQYLIEHGGDVNATDHTGQTALHWSAVRGAIQ 112
Cdd:COG0666  55 ALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLE 134

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230 113 VAELLLQEGARVDATDMYGYQATHVAAQYGQTAflchVVS---KWNADPDVPDNDGRSPLHWAAYKGFADSIRLLLFLDA 189
Cdd:COG0666 135 IVKLLLEAGADVNAQDNDGNTPLHLAAANGNLE----IVKlllEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA 210

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 79517230 190 YRGRQDKEGCTPLHWAAIRGNLEACTVLVQAGKkeDLMITDKTGLTPAQLAAEKNHRQVSFFLGNARSLLEKRCD 264
Cdd:COG0666 211 DVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA--DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
DHHC super family cl19890
DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which ...
 256-506 2.87e-28

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.


The actual alignment was detected with superfamily member COG5273:

Pssm-ID: 418707 [Multi-domain]  Cd Length: 309  Bit Score: 115.23  E-value: 2.87e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230 256 RSLLEKRCDGSSPLGRLSKLGLAP----------VLWIMILLLLLVYTNSVVLASNLPKLttgigalawlgFILATAgLF 325
Cdd:COG5273   4 KSWLPSTLGFIVFLVRLLRTGLYAykmfiglfllSRIVVYTLLVIVKSLSLVVLFIILFI-----------VILVLA-SF 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230 326 LFYRCSRKDPGYIRMNIHDPQTMKDDEPLLKIELNNpallagnWTQLCATCKIIRPLRAKHCSTCDRCVEQFDHHCPWVS 405
Cdd:COG5273  72 SYLLLLVSDPGYLGENITLSGYRETISRLLDDGKFG-------TENFCSTCNIYKPPRSHHCSICNRCVLKFDHHCPWIN 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230 406 NCVGKKN-KWEFFLFLLLEVLA--MLITGGVTLARVLSDPSAPSSfgAWMSHVASNHVGALSFLLVEFCLFFS-----VA 477
Cdd:COG5273 145 NCVGFRNyRFFYQFLLYTILVAlvVLLSTAYYIAGIFSIRHDTSL--AICFLIFGCSLLGVVFFIITTLLLLFliyliLN 222

                       250       260
                ....*....|....*....|....*....
gi 79517230 478 VLTVIQASQISRNITTNEMANALRYSYLR 506
Cdd:COG5273 223 NLTTIEFIQISRGGSTLEFFPLCRESNLP 251
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
33-264 2.77e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 148.56  E-value: 2.77e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230  33 NDVYTAAAYGDLEKLHRLVECEGSSVSEPDALGYYALQWSALNNRVAVAQYLIEHGGDVNATDHTGQTALHWSAVRGAIQ 112
Cdd:COG0666  55 ALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLE 134

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230 113 VAELLLQEGARVDATDMYGYQATHVAAQYGQTAflchVVS---KWNADPDVPDNDGRSPLHWAAYKGFADSIRLLLFLDA 189
Cdd:COG0666 135 IVKLLLEAGADVNAQDNDGNTPLHLAAANGNLE----IVKlllEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA 210

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 79517230 190 YRGRQDKEGCTPLHWAAIRGNLEACTVLVQAGKkeDLMITDKTGLTPAQLAAEKNHRQVSFFLGNARSLLEKRCD 264
Cdd:COG0666 211 DVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA--DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
COG5273 COG5273
Uncharacterized protein containing DHHC-type Zn finger [General function prediction only];
256-506 2.87e-28

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


Pssm-ID: 227598 [Multi-domain]  Cd Length: 309  Bit Score: 115.23  E-value: 2.87e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230 256 RSLLEKRCDGSSPLGRLSKLGLAP----------VLWIMILLLLLVYTNSVVLASNLPKLttgigalawlgFILATAgLF 325
Cdd:COG5273   4 KSWLPSTLGFIVFLVRLLRTGLYAykmfiglfllSRIVVYTLLVIVKSLSLVVLFIILFI-----------VILVLA-SF 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230 326 LFYRCSRKDPGYIRMNIHDPQTMKDDEPLLKIELNNpallagnWTQLCATCKIIRPLRAKHCSTCDRCVEQFDHHCPWVS 405
Cdd:COG5273  72 SYLLLLVSDPGYLGENITLSGYRETISRLLDDGKFG-------TENFCSTCNIYKPPRSHHCSICNRCVLKFDHHCPWIN 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230 406 NCVGKKN-KWEFFLFLLLEVLA--MLITGGVTLARVLSDPSAPSSfgAWMSHVASNHVGALSFLLVEFCLFFS-----VA 477
Cdd:COG5273 145 NCVGFRNyRFFYQFLLYTILVAlvVLLSTAYYIAGIFSIRHDTSL--AICFLIFGCSLLGVVFFIITTLLLLFliyliLN 222

                       250       260
                ....*....|....*....|....*....
gi 79517230 478 VLTVIQASQISRNITTNEMANALRYSYLR 506
Cdd:COG5273 223 NLTTIEFIQISRGGSTLEFFPLCRESNLP 251
DHHC pfam01529
DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which ...
 371-498 3.51e-27

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


Pssm-ID: 396215  Cd Length: 132  Bit Score: 106.68  E-value: 3.51e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230   371 QLCATCKIIRPLRAKHCSTCDRCVEQFDHHCPWVSNCVGKKN-K-------WefflfllleVLAMLITGGVTLARVLSDP 442
Cdd:pfam01529   6 KYCSTCNIYKPPRSKHCRVCNRCVLRFDHHCPWLNNCIGKRNhKyfilfllY---------LTLYLILYLVLSLYYLVKL 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 79517230   443 saPSSFGAWMSHVASNHVGALSFLLVEFCLFFSVAVLTVIQASQISRNITTNEMAN 498
Cdd:pfam01529  77 --IESSTLFFFLILFLFSISIILLILSLFFLLFLGILLFFHLYLISRNLTTYEFMK 130
Ank_2 pfam12796
Ankyrin repeats (3 copies);
136-230 2.33e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.38  E-value: 2.33e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230   136 HVAAQYGQTAFLCHVVSKwNADPDVPDNDGRSPLHWAAYKGFADSIRLLlfLDAYRGRQDKEGCTPLHWAAIRGNLEACT 215
Cdd:pfam12796   2 HLAAKNGNLELVKLLLEN-GADANLQDKNGRTALHLAAKNGHLEIVKLL--LEHADVNLKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|....*
gi 79517230   216 VLVQAGkkEDLMITD 230
Cdd:pfam12796  79 LLLEKG--ADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 55-252 5.31e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 80.84  E-value: 5.31e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230   55 GSSVSEPDALGYYALQWSALN-NRVAVAQYLIEHGGDVNATDHTGQTALH--WSAVRGAIQVAELLLQEGARVDATDMYG 131
Cdd:PHA03095  73 GADVNAPERCGFTPLHLYLYNaTTLDVIKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYG 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230  132 YQATHV------------------------AAQYGQTAFLCHVVS-KWNA-----------DPDVPDNDGRSPLHWAAYK 175
Cdd:PHA03095 153 MTPLAVllksrnanvellrllidagadvyaVDDRFRSLLHHHLQSfKPRArivreliragcDPAATDMLGNTPLHSMATG 232

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230  176 GFADSIRLLLFLDAyrG----RQDKEGCTPLHWAAIRGNLEACTVLVQAGkkEDLMITDKTGLTPAQLA-AEKNHRQVSF 250
Cdd:PHA03095 233 SSCKRSLVLPLLIA--GisinARNRYGQTPLHYAAVFNNPRACRRLIALG--ADINAVSSDGNTPLSLMvRNNNGRAVRA 308


                 ..
gi 79517230  251 FL 252
Cdd:PHA03095 309 AL 310
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 38-243 3.25e-11

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: 66.19  E-value: 3.25e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230  38 AAAYGDLEKLHRLVECEGSSVSEPDALGYYALQWSALNNRVAVAQYLIEHGGD-VN--ATD--HTGQTALHWSAVRGAIQ 112
Cdd:cd22192  24 AAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNepMTSdlYQGETALHIAVVNQNLN 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230 113 VAELLLQEGArvdatDMYGYQATHVAAQYGQTAfLCHVvskwnadpdvpdndGRSPLHWAAYKGFADSIRLLLFLDAYRG 192
Cdd:cd22192 104 LVRELIARGA-----DVVSPRATGTFFRPGPKN-LIYY--------------GEHPLSFAACVGNEEIVRLLIEHGADIR 163

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 79517230 193 RQDKEGCTPLHWAAIRGNLE-ACTV---LVQAGKKEDLM----ITDKTGLTPAQLAAEK 243
Cdd:cd22192 164 AQDSLGNTVLHILVLQPNKTfACQMydlILSYDKEDDLQpldlVPNNQGLTPFKLAAKE 222
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
33-264 2.77e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 148.56  E-value: 2.77e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230  33 NDVYTAAAYGDLEKLHRLVECEGSSVSEPDALGYYALQWSALNNRVAVAQYLIEHGGDVNATDHTGQTALHWSAVRGAIQ 112
Cdd:COG0666  55 ALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLE 134

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230 113 VAELLLQEGARVDATDMYGYQATHVAAQYGQTAflchVVS---KWNADPDVPDNDGRSPLHWAAYKGFADSIRLLLFLDA 189
Cdd:COG0666 135 IVKLLLEAGADVNAQDNDGNTPLHLAAANGNLE----IVKlllEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA 210

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 79517230 190 YRGRQDKEGCTPLHWAAIRGNLEACTVLVQAGKkeDLMITDKTGLTPAQLAAEKNHRQVSFFLGNARSLLEKRCD 264
Cdd:COG0666 211 DVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA--DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
38-302 1.81e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 138.16  E-value: 1.81e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230  38 AAAYGDLEKLHRLVECEGSSVSEPDALGYYALQWSALNNRVAVAQYLIEHGGDVNATDHTGQTALHWSAVRGAIQVAELL 117
Cdd:COG0666  27 AAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLL 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230 118 LQEGARVDATDMYGYQATHVAAQYGQTAFLCHVVSKwNADPDVPDNDGRSPLHWAAYKGFADSIRLLLFLDAYRGRQDKE 197
Cdd:COG0666 107 LEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA-GADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDND 185

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230 198 GCTPLHWAAIRGNLEACTVLVQAGKkeDLMITDKTGLTPAQLAAEKNHRQVSFFLGNARSLLEKRC-DGSSPLGRLSKLG 276
Cdd:COG0666 186 GETPLHLAAENGHLEIVKLLLEAGA--DVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDkDGLTALLLAAAAG 263

                       250       260
                ....*....|....*....|....*.
gi 79517230 277 LAPVLWIMILLLLLVYTNSVVLASNL 302
Cdd:COG0666 264 AALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
36-232 7.03e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 136.62  E-value: 7.03e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230  36 YTAAAYGDLEKLHRLVEcEGSSVSEPDALGYYALQWSALNNRVAVAQYLIEHGGDVNATDHTGQTALHWSAVRGAIQVAE 115
Cdd:COG0666  92 HAAARNGDLEIVKLLLE-AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230 116 LLLQEGARVDATDMYGYQATHVAAQYGQTAflchVVS---KWNADPDVPDNDGRSPLHWAAYKGFADSIRLLLFLDAYRG 192
Cdd:COG0666 171 LLLEAGADVNARDNDGETPLHLAAENGHLE----IVKlllEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 79517230 193 RQDKEGCTPLHWAAIRGNLEACTVLVQAGKKEDLMITDKT 232
Cdd:COG0666 247 AKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLL 286
COG5273 COG5273
Uncharacterized protein containing DHHC-type Zn finger [General function prediction only];
256-506 2.87e-28

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


Pssm-ID: 227598 [Multi-domain]  Cd Length: 309  Bit Score: 115.23  E-value: 2.87e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230 256 RSLLEKRCDGSSPLGRLSKLGLAP----------VLWIMILLLLLVYTNSVVLASNLPKLttgigalawlgFILATAgLF 325
Cdd:COG5273   4 KSWLPSTLGFIVFLVRLLRTGLYAykmfiglfllSRIVVYTLLVIVKSLSLVVLFIILFI-----------VILVLA-SF 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230 326 LFYRCSRKDPGYIRMNIHDPQTMKDDEPLLKIELNNpallagnWTQLCATCKIIRPLRAKHCSTCDRCVEQFDHHCPWVS 405
Cdd:COG5273  72 SYLLLLVSDPGYLGENITLSGYRETISRLLDDGKFG-------TENFCSTCNIYKPPRSHHCSICNRCVLKFDHHCPWIN 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230 406 NCVGKKN-KWEFFLFLLLEVLA--MLITGGVTLARVLSDPSAPSSfgAWMSHVASNHVGALSFLLVEFCLFFS-----VA 477
Cdd:COG5273 145 NCVGFRNyRFFYQFLLYTILVAlvVLLSTAYYIAGIFSIRHDTSL--AICFLIFGCSLLGVVFFIITTLLLLFliyliLN 222

                       250       260
                ....*....|....*....|....*....
gi 79517230 478 VLTVIQASQISRNITTNEMANALRYSYLR 506
Cdd:COG5273 223 NLTTIEFIQISRGGSTLEFFPLCRESNLP 251
DHHC pfam01529
DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which ...
 371-498 3.51e-27

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


Pssm-ID: 396215  Cd Length: 132  Bit Score: 106.68  E-value: 3.51e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230   371 QLCATCKIIRPLRAKHCSTCDRCVEQFDHHCPWVSNCVGKKN-K-------WefflfllleVLAMLITGGVTLARVLSDP 442
Cdd:pfam01529   6 KYCSTCNIYKPPRSKHCRVCNRCVLRFDHHCPWLNNCIGKRNhKyfilfllY---------LTLYLILYLVLSLYYLVKL 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 79517230   443 saPSSFGAWMSHVASNHVGALSFLLVEFCLFFSVAVLTVIQASQISRNITTNEMAN 498
Cdd:pfam01529  77 --IESSTLFFFLILFLFSISIILLILSLFFLLFLGILLFFHLYLISRNLTTYEFMK 130
Ank_2 pfam12796
Ankyrin repeats (3 copies);
136-230 2.33e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.38  E-value: 2.33e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230   136 HVAAQYGQTAFLCHVVSKwNADPDVPDNDGRSPLHWAAYKGFADSIRLLlfLDAYRGRQDKEGCTPLHWAAIRGNLEACT 215
Cdd:pfam12796   2 HLAAKNGNLELVKLLLEN-GADANLQDKNGRTALHLAAKNGHLEIVKLL--LEHADVNLKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|....*
gi 79517230   216 VLVQAGkkEDLMITD 230
Cdd:pfam12796  79 LLLEKG--ADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
84-269 3.24e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 79.61  E-value: 3.24e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230  84 LIEHGGDVNATDHTGQTALHWSAVRGAIQVAELLLQEGARVDATDMYGYQATHVAAQYGQTAFLCHVVSKWNADPDVPDN 163
Cdd:COG0666   6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230 164 DGRSPLHWAAYKGFADSIRLLLFLDAYRGRQDKEGCTPLHWAAIRGNLEACTVLVQAGkkEDLMITDKTGLTPAQLAAEK 243
Cdd:COG0666  86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAG--ADVNAQDNDGNTPLHLAAAN 163

                       170       180       190
                ....*....|....*....|....*....|...
gi 79517230 244 NHRQVsfflgnARSLLEKRCD-------GSSPL 269
Cdd:COG0666 164 GNLEI------VKLLLEAGADvnardndGETPL 190
Ank_2 pfam12796
Ankyrin repeats (3 copies);
38-128 3.51e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.00  E-value: 3.51e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230    38 AAAYGDLEKLHRLVECeGSSVSEPDALGYYALQWSALNNRVAVAQYLIEHgGDVNATDHtGQTALHWSAVRGAIQVAELL 117
Cdd:pfam12796   4 AAKNGNLELVKLLLEN-GADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLL 80

                          90
                  ....*....|.
gi 79517230   118 LQEGARVDATD 128
Cdd:pfam12796  81 LEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 55-252 5.31e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 80.84  E-value: 5.31e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230   55 GSSVSEPDALGYYALQWSALN-NRVAVAQYLIEHGGDVNATDHTGQTALH--WSAVRGAIQVAELLLQEGARVDATDMYG 131
Cdd:PHA03095  73 GADVNAPERCGFTPLHLYLYNaTTLDVIKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYG 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230  132 YQATHV------------------------AAQYGQTAFLCHVVS-KWNA-----------DPDVPDNDGRSPLHWAAYK 175
Cdd:PHA03095 153 MTPLAVllksrnanvellrllidagadvyaVDDRFRSLLHHHLQSfKPRArivreliragcDPAATDMLGNTPLHSMATG 232

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230  176 GFADSIRLLLFLDAyrG----RQDKEGCTPLHWAAIRGNLEACTVLVQAGkkEDLMITDKTGLTPAQLA-AEKNHRQVSF 250
Cdd:PHA03095 233 SSCKRSLVLPLLIA--GisinARNRYGQTPLHYAAVFNNPRACRRLIALG--ADINAVSSDGNTPLSLMvRNNNGRAVRA 308


                 ..
gi 79517230  251 FL 252
Cdd:PHA03095 309 AL 310
Ank_2 pfam12796
Ankyrin repeats (3 copies);
169-264 2.25e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.99  E-value: 2.25e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230   169 LHWAAYKGFADSIRLLLFLDAYRGRQDKEGCTPLHWAAIRGNLEACTVLVqagKKEDLMITDKtGLTPAQLAAEKNHRQV 248
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL---EHADVNLKDN-GRTALHYAARSGHLEI 76

                          90
                  ....*....|....*.
gi 79517230   249 sfflgnARSLLEKRCD 264
Cdd:pfam12796  77 ------VKLLLEKGAD 86
Ank_2 pfam12796
Ankyrin repeats (3 copies);
69-162 4.61e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.14  E-value: 4.61e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230    69 LQWSALNNRVAVAQYLIEHGGDVNATDHTGQTALHWSAVRGAIQVAELLLQEgARVDATDmYGYQATHVAAQYGQTAFLC 148
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|....
gi 79517230   149 HVVSKwNADPDVPD 162
Cdd:pfam12796  79 LLLEK-GADINVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 65-252 2.43e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 69.25  E-value: 2.43e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230   65 GYYALQWSALNNRVAVAQYLIEHGGDVNATDHTGQTALHWSAVRGAIQVAELLLQEGARVDatDMY---GYQATHVAAQY 141
Cdd:PHA02875  35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAD--DVFykdGMTPLHLATIL 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230  142 gQTAFLCHVVSKWNADPDVPDNDGRSPLHWAAYKGFADSIRLLLFLDAYRGRQDKEGCTPLHWAAIRGNLEACTVLVQAG 221
Cdd:PHA02875 113 -KKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSG 191

                        170       180       190
                 ....*....|....*....|....*....|...
gi 79517230  222 KKEDLMitDKTGLTPAQLAAEKNHR--QVSFFL 252
Cdd:PHA02875 192 ANIDYF--GKNGCVAALCYAIENNKidIVRLFI 222
PHA03095 PHA03095
ankyrin-like protein; Provisional
 75-224 1.51e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 66.97  E-value: 1.51e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230   75 NNRVAVAQYLIEHGGDVNATDHTGQTALHWSAVRGAIQVAE---LLLQEGARVDATDMYGYQATHVAAQYGQTAFLCHVV 151
Cdd:PHA03095  24 NVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDivrLLLEAGADVNAPERCGFTPLHLYLYNATTLDVIKLL 103

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79517230  152 SKWNADPDVPDNDGRSPLHwaAY-KGF---ADSIRLLLFLDAYRGRQDKEGCTPLHWAAIRGNLEACTV--LVQAGKKE 224
Cdd:PHA03095 104 IKAGADVNAKDKVGRTPLH--VYlSGFninPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVELLrlLIDAGADV 180
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 38-243 3.25e-11

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: 66.19  E-value: 3.25e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230  38 AAAYGDLEKLHRLVECEGSSVSEPDALGYYALQWSALNNRVAVAQYLIEHGGD-VN--ATD--HTGQTALHWSAVRGAIQ 112
Cdd:cd22192  24 AAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNepMTSdlYQGETALHIAVVNQNLN 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230 113 VAELLLQEGArvdatDMYGYQATHVAAQYGQTAfLCHVvskwnadpdvpdndGRSPLHWAAYKGFADSIRLLLFLDAYRG 192
Cdd:cd22192 104 LVRELIARGA-----DVVSPRATGTFFRPGPKN-LIYY--------------GEHPLSFAACVGNEEIVRLLIEHGADIR 163

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 79517230 193 RQDKEGCTPLHWAAIRGNLE-ACTV---LVQAGKKEDLM----ITDKTGLTPAQLAAEK 243
Cdd:cd22192 164 AQDSLGNTVLHILVLQPNKTfACQMydlILSYDKEDDLQpldlVPNNQGLTPFKLAAKE 222
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 43-240 1.33e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 63.83  E-value: 1.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230   43 DLEK--LHRLVECeGSSVSEPDALGYYALQWSALNNRVAVAQYLIEHGGDVNATDHTGQTALHWSAVRGAIQVAELLLQE 120
Cdd:PHA02874 101 CIEKdmIKTILDC-GIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEK 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230  121 GARVDATDMYGYQATHVAAQYGQTAFLCHVVSKWNaDPDVPDNDGRSPLHWAAYkgFADSIRLLLFLDAYRGRQDKEGCT 200
Cdd:PHA02874 180 GAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGN-HIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGST 256

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 79517230  201 PLHWaAIRGNLEACTVLVQAGKKEDLMITDKTGLTPAQLA 240
Cdd:PHA02874 257 PLHH-AINPPCDIDIIDILLYHKADISIKDNKGENPIDTA 295
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 66-229 4.74e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 61.99  E-value: 4.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230   66 YYALQWSALNNRVAVAQYLIEHGGDVNATDHTGQTALHWSAVR--GAIQVAELLLQEGARVDATDMYGYQATHVAAQYGQ 143
Cdd:PHA03100  74 YLSNIKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNK 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230  144 TA------FLCHVVS-----------KWNADPDVPDNDGRSPLHWAAYKGFADSIRLLLFLDAYRGRQDKEGCTPLHWAA 206
Cdd:PHA03100 154 IDlkilklLIDKGVDinaknrvnyllSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAI 233

                        170       180
                 ....*....|....*....|...
gi 79517230  207 IRGNLEACTVLVQAGKKEDLMIT 229
Cdd:PHA03100 234 LNNNKEIFKLLLNNGPSIKTIIE 256
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 34-269 9.80e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 61.13  E-value: 9.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230   34 DVYTAAAYGDLEKLHRLVECEGS----SVSEPDALGYYALQwsalNNRVAVAQYLIEHGGDVNATDHTGQTALHWSAVRG 109
Cdd:PHA02874   4 DLRMCIYSGDIEAIEKIIKNKGNciniSVDETTTPLIDAIR----SGDAKIVELFIKHGADINHINTKIPHPLLTAIKIG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230  110 AIQVAELL-----------------------LQEGARVDATDMYGYQATHVAAQYGQTAFLcHVVSKWNADPDVPDNDGR 166
Cdd:PHA02874  80 AHDIIKLLidngvdtsilpipciekdmiktiLDCGIDVNIKDAELKTFLHYAIKKGDLESI-KMLFEYGADVNIEDDNGC 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230  167 SPLHWAAYKGFADSIRLLLFLDAYRGRQDKEGCTPLHWAAIRGNLEACTVLVQAGKkeDLMITDKTGLTPAQLAAEKNhR 246
Cdd:PHA02874 159 YPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGN--HIMNKCKNGFTPLHNAIIHN-R 235

                        250       260
                 ....*....|....*....|...
gi 79517230  247 QVSFFLGNARSLLEKRCDGSSPL 269
Cdd:PHA02874 236 SAIELLINNASINDQDIDGSTPL 258
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
116-269 2.05e-08

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 56.12  E-value: 2.05e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230 116 LLLQEGARVDATDMYGYQATHVAAQYGQTAFLCHVVSKWNADPDVPDNDGRSPLHWAAYKGFADSIRLLLFLDAYRGRQD 195
Cdd:COG0666   5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230 196 KEGCTPLHWAAIRGNLEACTVLVQAGkkEDLMITDKTGLTPAQLAAEKNHRQVsfflgnARSLLEKRCD-------GSSP 268
Cdd:COG0666  85 DGGNTLLHAAARNGDLEIVKLLLEAG--ADVNARDKDGETPLHLAAYNGNLEI------VKLLLEAGADvnaqdndGNTP 156


                .
gi 79517230 269 L 269
Cdd:COG0666 157 L 157
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 76-245 3.44e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 52.75  E-value: 3.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230   76 NRVAVAQYLIEHGGDVNATDHTGQTALHWSAVRGAIQ-----VAELLLQEGARVDATDMYGYQATHVAAqygqTAFLCHV 150
Cdd:PHA03100  46 RNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLtdvkeIVKLLLEYGANVNAPDNNGITPLLYAI----SKKSNSY 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230  151 -----VSKWNADPDVPDNDGRSPLHWAA--------------YKGF----ADSIRLLLFLDAYRGRQDKEGCTPLHWAAI 207
Cdd:PHA03100 122 siveyLLDNGANVNIKNSDGENLLHLYLesnkidlkilklliDKGVdinaKNRVNYLLSYGVPINIKDVYGFTPLHYAVY 201

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 79517230  208 RGNLEACTVLVQAGKkeDLMITDKTGLTPAQLAAEKNH 245
Cdd:PHA03100 202 NNNPEFVKYLLDLGA--NPNLVNKYGDTPLHIAILNNN 237
Ank_4 pfam13637
Ankyrin repeats (many copies);
68-118 3.90e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.27  E-value: 3.90e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 79517230    68 ALQWSALNNRVAVAQYLIEHGGDVNATDHTGQTALHWSAVRGAIQVAELLL 118
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
165-218 5.44e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.50  E-value: 5.44e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 79517230   165 GRSPLHWAAYKGFADSIRLLL--FLDAYRgrQDKEGCTPLHWAAIRGNLEACTVLV 218
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLekGADINA--VDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 80-205 1.04e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 51.42  E-value: 1.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230   80 VAQYLIEHGGDVNATD-HTGQTALHWSAVRGAIQVAELLLQEGarvdatdmygyqathvaaqygqtaflchvvskwnADP 158
Cdd:PHA02878 149 ITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYG----------------------------------ANV 194

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 79517230  159 DVPDNDGRSPLHWAAYKGFADSIRLLLFLDAYRGRQDKEGCTPLHWA 205
Cdd:PHA02878 195 NIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIS 241
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 22-185 3.55e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 50.06  E-value: 3.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230   22 SSKGIEEESlknDVYTAAAYG-DLEKLHRLVEcEGSSVSEPDALGYYAL-QWSALNNRVAVAQYLIEHGGDVNATDHTGQ 99
Cdd:PHA02876 301 NAKNIKGET---PLYLMAKNGyDTENIRTLIM-LGADVNAADRLYITPLhQASTLDRNKDIVITLLELGANVNARDYCDK 376

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230  100 TALHWSAVRGAIQVAELLLQEGARVDATDMYGYQATHVAAqYGQTAFL-CHVVSKWNADPDVPDNDGRSPLHWAAYKGFA 178
Cdd:PHA02876 377 TPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAL-CGTNPYMsVKTLIDRGANVNSKNKDLSTPLHYACKKNCK 455


                 ....*...
gi 79517230  179 -DSIRLLL 185
Cdd:PHA02876 456 lDVIEMLL 463
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 75-221 2.14e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 47.75  E-value: 2.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230   75 NNRVAVAQYLIEHGGDVNATDHTGQTALHWSAVRGAI-QVAELLLQEGARVDATDMYGYQATHVAAQYGQTAFLCHVVSK 153
Cdd:PHA02876 250 NEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAKNGYDTENIRTLIM 329

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79517230  154 WNADPDVPDNDGRSPLHWAA-YKGFADSIRLLLFLDAYRGRQDKEGCTPLHWAAIRGNLEACTVLVQAG 221
Cdd:PHA02876 330 LGADVNAADRLYITPLHQAStLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYG 398
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 173-248 2.63e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.20  E-value: 2.63e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79517230  173 AYKGFADSIRLLLFLDAYRGRQDKEGCTPLHWAAIRGNLEACTVLVQAGKkeDLMITDKTGLTPAQLAAEKNHRQV 248
Cdd:PTZ00322  90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGA--DPTLLDKDGKTPLELAEENGFREV 163
Ank_4 pfam13637
Ankyrin repeats (many copies);
200-252 3.14e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.88  E-value: 3.14e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 79517230   200 TPLHWAAIRGNLEACTVLVQAGKkeDLMITDKTGLTPAQLAAEKNHRQVSFFL 252
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGA--DINAVDGNGETALHFAASNGNVEVLKLL 53
Ank_5 pfam13857
Ankyrin repeats (many copies);
193-240 3.82e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.56  E-value: 3.82e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 79517230   193 RQDKEGCTPLHWAAIRGNLEACTVLVQAGkkEDLMITDKTGLTPAQLA 240
Cdd:pfam13857  11 RLDGEGYTPLHVAAKYGALEIVRVLLAYG--VDLNLKDEEGLTALDLA 56
PHA02946 PHA02946
ankyin-like protein; Provisional
 45-202 4.25e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 46.20  E-value: 4.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230   45 EKLHRlveceGSSVSEPDALGYYALQWSALNNRVAVAQYLIEHGGDVNATDHTGQTALHWSAVRG--AIQVAELLLQEGA 122
Cdd:PHA02946  57 ELLHR-----GYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDdeVIERINLLVQYGA 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230  123 RVD-------------ATD----------MYGYQAtHVAAQYGQTAFLCHVVS------------KWNADPDVPDNDGRS 167
Cdd:PHA02946 132 KINnsvdeegcgpllaCTDpservfkkimSIGFEA-RIVDKFGKNHIHRHLMSdnpkastiswmmKLGISPSKPDHDGNT 210

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 79517230  168 PLHWAAYKGFAD-SIRLLLFLDAYRGRQDKEGCTPL 202
Cdd:PHA02946 211 PLHIVCSKTVKNvDIINLLLPSTDVNKQNKFGDSPL 246
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 81-185 4.73e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.43  E-value: 4.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230   81 AQYLIEHGGDVNATDHTGQTALHWSAVRGAIQVAELLLQEGarvdatdmygyqathvaaqygqtaflchvvskwnADPDV 160
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFG----------------------------------ADPTL 143

                         90       100
                 ....*....|....*....|....*
gi 79517230  161 PDNDGRSPLHWAAYKGFADSIRLLL 185
Cdd:PTZ00322 144 LDKDGKTPLELAEENGFREVVQLLS 168
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 111-252 5.81e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 46.40  E-value: 5.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230  111 IQVAELLLQEGARVDATDMYGYQAThvAAQYGQTAFLCHVVsKWNADPDVPDNDGRSPLHWAAYKGFADSIRLLLFLDAY 190
Cdd:PLN03192 507 LNVGDLLGDNGGEHDDPNMASNLLT--VASTGNAALLEELL-KAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACN 583

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230  191 RGRQDKEGCTPL----------------HWAAIRGNLEACTVLVQAGKKEDLMI-------------TDKTGLTPAQLAA 241
Cdd:PLN03192 584 VHIRDANGNTALwnaisakhhkifrilyHFASISDPHAAGDLLCTAAKRNDLTAmkellkqglnvdsEDHQGATALQVAM 663

                        170
                 ....*....|.
gi 79517230  242 EKNHRQVSFFL 252
Cdd:PLN03192 664 AEDHVDMVRLL 674
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 46-169 9.97e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 45.26  E-value: 9.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230   46 KLHRLVECEGSSVSEPDALGYYALQWSALNNRVAVAQYLIEHGGDVNATDHTGQTALHWSAVR-GAIQVAELLLQEGARV 124
Cdd:PHA02878 182 RLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDV 261

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 79517230  125 DA-TDMYGYQATHVAAQYGQTAFLchvVSKWNADPDVPDNDGRSPL 169
Cdd:PHA02878 262 NAkSYILGLTALHSSIKSERKLKL---LLEYGADINSLNSYKLTPL 304
PHA03095 PHA03095
ankyrin-like protein; Provisional
 54-151 1.44e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 44.63  E-value: 1.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230   54 EGSSVSEPDALGYYALQWSA-LNNRVAVAqYLIEHGGDVNATDHTGQTAL-------HWSAVRGAIQ------------- 112
Cdd:PHA03095 246 AGISINARNRYGQTPLHYAAvFNNPRACR-RLIALGADINAVSSDGNTPLslmvrnnNGRAVRAALAknpsaetvaatln 324

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 79517230  113 -----------------VAELLLQEGARVDATDMYGYQATHVAAQYGQTAFLCHVV 151
Cdd:PHA03095 325 tasvaggdipsdatrlcVAKVVLRGAFSLLPEPIRAYHADFIRECEAEIAVMRTTR 380
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 111-276 2.23e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 44.28  E-value: 2.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230  111 IQVAELLLQEGARVDATDMYGYQATHVAAQYGQTAFLCHVVSkWNADPDVPDNDGRSPLHWAAYKGFADSIRLLLfldAY 190
Cdd:PHA02876 158 LLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLS-YGADVNIIALDDLSVLECAVDSKNIDTIKAII---DN 233

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230  191 RGRQDKEGCTPLHwaAIRG-NLEACTVLVQAGKKEDLMitDKTGLTPAQLAAEKN--HRQVSFFLGNARSLLEKRCDGSS 267
Cdd:PHA02876 234 RSNINKNDLSLLK--AIRNeDLETSLLLYDAGFSVNSI--DDCKNTPLHHASQAPslSRLVPKLLERGADVNAKNIKGET 309


                 ....*....
gi 79517230  268 PLGRLSKLG 276
Cdd:PHA02876 310 PLYLMAKNG 318
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 56-130 2.35e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 44.47  E-value: 2.35e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 79517230   56 SSVSEPDALGYyALQWSALNNRVAVAQYLIEHGGDVNATDHTGQTALHWSAVRGAIQVAELLLQEGARVDATDMY 130
Cdd:PLN03192 614 ASISDPHAAGD-LLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTD 687
Ank_5 pfam13857
Ankyrin repeats (many copies);
84-138 2.35e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.25  E-value: 2.35e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 79517230    84 LIEHGG-DVNATDHTGQTALHWSAVRGAIQVAELLLQEGARVDATDMYGYQATHVA 138
Cdd:pfam13857   1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 38-176 2.38e-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: 44.23  E-value: 2.38e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230  38 AAAYGDLEKLHRLVECEGSSVSEPDA----LGYYALQWSALNNRVAVAQYLIEHGGDVN---ATD-----------HTGQ 99
Cdd:cd22192  58 AALYDNLEAAVVLMEAAPELVNEPMTsdlyQGETALHIAVVNQNLNLVRELIARGADVVsprATGtffrpgpknliYYGE 137

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230 100 TALHWSAVRGAIQVAELLLQEGARVDATDMYGYQATHVAAQYGQTAFLCHVV-----SKWNADP----DVPDNDGRSPLH 170
Cdd:cd22192 138 HPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFACQMYdlilsYDKEDDLqpldLVPNNQGLTPFK 217


                ....*.
gi 79517230 171 WAAYKG 176
Cdd:cd22192 218 LAAKEG 223
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 68-141 2.43e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 44.10  E-value: 2.43e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79517230   68 ALQWSALNNRVAVAQYLIEHGGDVNATDHTGQTALHWSAVRGAIQVAELLLQEGARVDATDMYGYQATHVAAQY 141
Cdd:PHA02878 171 ALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGY 244
Ank_5 pfam13857
Ankyrin repeats (many copies);
155-205 3.04e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.87  E-value: 3.04e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 79517230   155 NADPDVPDNDGRSPLHWAAYKGFADSIRLLLFLDAYRGRQDKEGCTPLHWA 205
Cdd:pfam13857   6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
38-85 4.04e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.41  E-value: 4.04e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 79517230    38 AAAYGDLEKLHRLVEcEGSSVSEPDALGYYALQWSALNNRVAVAQYLI 85
Cdd:pfam13637   8 AAASGHLELLRLLLE-KGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
100-147 4.46e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.41  E-value: 4.46e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 79517230   100 TALHWSAVRGAIQVAELLLQEGARVDATDMYGYQATHVAAQYGQTAFL 147
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVL 50
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 98-128 7.26e-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: 37.27  E-value: 7.26e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 79517230    98 GQTALHWSAVR-GAIQVAELLLQEGARVDATD 128
Cdd:pfam00023   2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
Ank_2 pfam12796
Ankyrin repeats (3 copies);
36-95 8.14e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 38.94  E-value: 8.14e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230    36 YTAAAYGDLEKLHRLVECEgssVSEPDALGYYALQWSALNNRVAVAQYLIEHGGDVNATD 95
Cdd:pfam12796  35 HLAAKNGHLEIVKLLLEHA---DVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 156-205 8.68e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.19  E-value: 8.68e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 79517230  156 ADPDVPDNDGRSPLHWAAYKGFADSIRLLLFLDAYRGRQDKEGCTPLHWA 205
Cdd:PTZ00322 106 ADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA 155
Ank_5 pfam13857
Ankyrin repeats (many copies);
50-103 1.15e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.33  E-value: 1.15e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 79517230    50 LVECEGSSVSEPDALGYYALQWSALNNRVAVAQYLIEHGGDVNATDHTGQTALH 103
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 45-128 2.27e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 40.78  E-value: 2.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230   45 EKLHRLVEcEGSSVSEPDALGYYALQWSALNN--RVAVAQYLIEHGGDVNATDHTGQTALHWSAVRGAIQVAELLLQEGA 122
Cdd:PHA03095 203 RIVRELIR-AGCDPAATDMLGNTPLHSMATGSscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGA 281


                 ....*.
gi 79517230  123 RVDATD 128
Cdd:PHA03095 282 DINAVS 287
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 76-244 2.28e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 41.20  E-value: 2.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230   76 NRVAVAQYLIEHGGDVNATDHTGQTALHWSAVRGAIQVAELLLQEGA--------------------------------- 122
Cdd:PHA02876 156 DELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGAdvniialddlsvlecavdsknidtikaiidnrs 235

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230  123 -----------------------------RVDATDMYGYQATHVAAQYGQTAFLCHVVSKWNADPDVPDNDGRSPLHWAA 173
Cdd:PHA02876 236 ninkndlsllkairnedletslllydagfSVNSIDDCKNTPLHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMA 315

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79517230  174 YKGF-ADSIRLLLFLDAYRGRQDKEGCTPLHWAA-IRGNLEACTVLVQAGKkeDLMITDKTGLTPAQLAAEKN 244
Cdd:PHA02876 316 KNGYdTENIRTLIMLGADVNAADRLYITPLHQAStLDRNKDIVITLLELGA--NVNARDYCDKTPIHYAAVRN 386
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 55-130 2.77e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 40.42  E-value: 2.77e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79517230   55 GSSVSEPDALGYYALQWSALNNRVAVAQYLIEHGGDVNATDHTGQTALHWSAVRGAIQVAELLLQEGARVDATDMY 130
Cdd:PHA03100 182 GVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 65-172 3.76e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 40.25  E-value: 3.76e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517230  65 GYYALQWSALNNRVAVAQYLIEHGGD---VNATDHTGQTALH---------WSAVRGAIQVAELLLQEGARVDAT----- 127
Cdd:cd21882 119 GELPLSLAACTNQEEIVRLLLENGAQpaaLEAQDSLGNTVLHalvlqadntPENSAFVCQMYNLLLSYGAHLDPTqqlee 198

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 79517230 128 --DMYGYQATHVAAQYGQTAFLCHVVSKWNADPDVPDNdgRSPLHWA 172
Cdd:cd21882 199 ipNHQGLTPLKLAAVEGKIVMFQHILQREFSGPYQPLS--RKFTEWT 243
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 65-93 5.03e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.93  E-value: 5.03e-03
                          10        20
                  ....*....|....*....|....*....
gi 79517230    65 GYYALQWSALNNRVAVAQYLIEHGGDVNA 93
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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