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Conserved domains on  [gi|1327850424|ref|NP_001346555|]
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palmitoyltransferase ZDHHC17 isoform 2 [Homo sapiens]

Protein Classification

ankyrin repeat domain-containing DHHC palmitoyltransferase family protein( domain architecture ID 12790884)

DHHC family palmitoyltransferase may catalyze the addition of palmitate onto various protein substrates and be involved in a variety of cellular processes; contains N-terminal ankyrin repeats;

EC:  2.3.1.-
Gene Ontology:  GO:0043543|GO:0016747
PubMed:  21388813

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
42-297 8.71e-46

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 163.97  E-value: 8.71e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424  42 HIDDYSTWDIVKATQYGIYERCRELVEAGYDVRQPDKENVTLLHWAAINNRIDLVKYYISKGAIVDQLGGDLNsTPLHWA 121
Cdd:COG0666    16 LLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGN-TLLHAA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424 122 TRQGHLSMVVQLMKYGADPSLIDGEGCSCIHLAAQFGHTSIVAYLIAKGQDVDMMDQNGMTPLMWAAYRTHsVDPTRLLL 201
Cdd:COG0666    95 ARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN-LEIVKLLL 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424 202 TFNVSVNLGDKYhKNTALHWAVLAGNTTVISLLLEAGANVDAQNIKGESALDLAKQRKNVWMINHLQEARQAKGYDNPSF 281
Cdd:COG0666   174 EAGADVNARDND-GETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDG 252

                         250
                  ....*....|....*.
gi 1327850424 282 LRKLKADKEFRQKVML 297
Cdd:COG0666   253 LTALLLAAAAGAALIV 268
DHHC pfam01529
DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which ...
 428-558 2.49e-40

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: 143.28  E-value: 2.49e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424 428 FCSTCLIRKPVRSKHCGVCNRCIAKFDHHCPWVGNCVGAGNHRYFMGYLFFLLFMICWMIYGCISYWGLHCETTYTKDGF 507
Cdd:pfam01529   7 YCSTCNIYKPPRSKHCRVCNRCVLRFDHHCPWLNNCIGKRNHKYFILFLLYLTLYLILYLVLSLYYLVKLIESSTLFFFL 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1327850424 508 WTYITQiatcspWMFWMFLNSVFHFMWVAVLLMCQMYQIsCLGITTNERMN 558
Cdd:pfam01529  87 ILFLFS------ISIILLILSLFFLLFLGILLFFHLYLI-SRNLTTYEFMK 130
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
42-297 8.71e-46

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 163.97  E-value: 8.71e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424  42 HIDDYSTWDIVKATQYGIYERCRELVEAGYDVRQPDKENVTLLHWAAINNRIDLVKYYISKGAIVDQLGGDLNsTPLHWA 121
Cdd:COG0666    16 LLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGN-TLLHAA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424 122 TRQGHLSMVVQLMKYGADPSLIDGEGCSCIHLAAQFGHTSIVAYLIAKGQDVDMMDQNGMTPLMWAAYRTHsVDPTRLLL 201
Cdd:COG0666    95 ARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN-LEIVKLLL 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424 202 TFNVSVNLGDKYhKNTALHWAVLAGNTTVISLLLEAGANVDAQNIKGESALDLAKQRKNVWMINHLQEARQAKGYDNPSF 281
Cdd:COG0666   174 EAGADVNARDND-GETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDG 252

                         250
                  ....*....|....*.
gi 1327850424 282 LRKLKADKEFRQKVML 297
Cdd:COG0666   253 LTALLLAAAAGAALIV 268
DHHC pfam01529
DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which ...
 428-558 2.49e-40

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: 143.28  E-value: 2.49e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424 428 FCSTCLIRKPVRSKHCGVCNRCIAKFDHHCPWVGNCVGAGNHRYFMGYLFFLLFMICWMIYGCISYWGLHCETTYTKDGF 507
Cdd:pfam01529   7 YCSTCNIYKPPRSKHCRVCNRCVLRFDHHCPWLNNCIGKRNHKYFILFLLYLTLYLILYLVLSLYYLVKLIESSTLFFFL 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1327850424 508 WTYITQiatcspWMFWMFLNSVFHFMWVAVLLMCQMYQIsCLGITTNERMN 558
Cdd:pfam01529  87 ILFLFS------ISIILLILSLFFLLFLGILLFFHLYLI-SRNLTTYEFMK 130
COG5273 COG5273
Uncharacterized protein containing DHHC-type Zn finger [General function prediction only];
348-547 2.29e-33

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


Pssm-ID: 227598 [Multi-domain]  Cd Length: 309  Bit Score: 129.87  E-value: 2.29e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424 348 LPLGIYLATKFWMYVTWFFWFWNDLNFLFIHLPFLANSVALFYnFGKSWKSDPGII--KATEEQKKKTIVELAETGSLDL 425
Cdd:COG5273    30 MFIGLFLLSRIVVYTLLVIVKSLSLVVLFIILFIVILVLASFS-YLLLLVSDPGYLgeNITLSGYRETISRLLDDGKFGT 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424 426 SIFCSTCLIRKPVRSKHCGVCNRCIAKFDHHCPWVGNCVGAGNHRYFMGYLFFLLFMICWMIYGCISY----WGLHCETT 501
Cdd:COG5273   109 ENFCSTCNIYKPPRSHHCSICNRCVLKFDHHCPWINNCVGFRNYRFFYQFLLYTILVALVVLLSTAYYiagiFSIRHDTS 188

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1327850424 502 YTKD-----------GFWTYITqiatcspwMFWMFLNsvfhFMWVAVLLMCQMYQIS 547
Cdd:COG5273   189 LAICflifgcsllgvVFFIITT--------LLLLFLI----YLILNNLTTIEFIQIS 233
Ank_2 pfam12796
Ankyrin repeats (3 copies);
151-245 4.05e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.95  E-value: 4.05e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424 151 IHLAAQFGHTSIVAYLIAKGQDVDMMDQNGMTPLMWAAYRTHsVDPTRLLLTFnvsVNLGDKYHKNTALHWAVLAGNTTV 230
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGH-LEIVKLLLEH---ADVNLKDNGRTALHYAARSGHLEI 76

                          90
                  ....*....|....*
gi 1327850424 231 ISLLLEAGANVDAQN 245
Cdd:pfam12796  77 VKLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 42-267 3.24e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 81.25  E-value: 3.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424  42 HIDDYSTWDIVKATQYGIYERCRELVEA----GYDVRQPDKENVTLLHWAA-----INNRIDLVKYYISKGAIVDQlGGD 112
Cdd:PHA03100   26 DLNDYSYKKPVLPLYLAKEARNIDVVKIlldnGADINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLEYGANVNA-PDN 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424 113 LNSTPLHWA--TRQGHLSMVVQLMKYGADPSLIDGEGCSCIHLAAQFGH--TSIVAYLIAKGQDVDMMDqngmtplmwaa 188
Cdd:PHA03100  105 NGITPLLYAisKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKN----------- 173

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1327850424 189 yrthSVDptrLLLTFNVSVNLGDKYHkNTALHWAVLAGNTTVISLLLEAGANVDAQNIKGESALDLAKQRKNVWMINHL 267
Cdd:PHA03100  174 ----RVN---YLLSYGVPINIKDVYG-FTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLL 244
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 214-243 1.75e-04

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: 39.11  E-value: 1.75e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1327850424  214 HKNTALHWAVLAGNTTVISLLLEAGANVDA 243
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 82-271 1.37e-03

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 41.54  E-value: 1.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424  82 TLLHWAAINNRIDLVKYYI--SKGAIVDQLGGDL--NSTPLHWATRQGHLSMVVQLMKYGADPS--------LIDGEGCS 149
Cdd:cd22192    53 TALHVAALYDNLEAAVVLMeaAPELVNEPMTSDLyqGETALHIAVVNQNLNLVRELIARGADVVspratgtfFRPGPKNL 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424 150 C------IHLAAQFGHTSIVAYLIAKGQDVDMMDQNGmtplmwaayrthsvdptrllltfnvsvnlgdkyhkNTALHWAV 223
Cdd:cd22192   133 IyygehpLSFAACVGNEEIVRLLIEHGADIRAQDSLG-----------------------------------NTVLHILV 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1327850424 224 LAGNTT----VISLLLEAGANVDAQ------NIKGESALDLAKQRKNVWMINHLQEAR 271
Cdd:cd22192   178 LQPNKTfacqMYDLILSYDKEDDLQpldlvpNNQGLTPFKLAAKEGNIVMFQHLVQKR 235
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
42-297 8.71e-46

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 163.97  E-value: 8.71e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424  42 HIDDYSTWDIVKATQYGIYERCRELVEAGYDVRQPDKENVTLLHWAAINNRIDLVKYYISKGAIVDQLGGDLNsTPLHWA 121
Cdd:COG0666    16 LLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGN-TLLHAA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424 122 TRQGHLSMVVQLMKYGADPSLIDGEGCSCIHLAAQFGHTSIVAYLIAKGQDVDMMDQNGMTPLMWAAYRTHsVDPTRLLL 201
Cdd:COG0666    95 ARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN-LEIVKLLL 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424 202 TFNVSVNLGDKYhKNTALHWAVLAGNTTVISLLLEAGANVDAQNIKGESALDLAKQRKNVWMINHLQEARQAKGYDNPSF 281
Cdd:COG0666   174 EAGADVNARDND-GETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDG 252

                         250
                  ....*....|....*.
gi 1327850424 282 LRKLKADKEFRQKVML 297
Cdd:COG0666   253 LTALLLAAAAGAALIV 268
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
44-285 1.05e-44

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 160.89  E-value: 1.05e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424  44 DDYSTWDIVKATQYGIYERCRELVEAGYDVRQPDKENVTLLHWAAINNRIDLVKYYISKGAIVDQLGGDLNsTPLHWATR 123
Cdd:COG0666    51 DALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGE-TPLHLAAY 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424 124 QGHLSMVVQLMKYGADPSLIDGEGCSCIHLAAQFGHTSIVAYLIAKGQDVDMMDQNGMTPLMWAAYRTHsVDPTRLLLTF 203
Cdd:COG0666   130 NGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGH-LEIVKLLLEA 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424 204 NVSVNLGDKYHkNTALHWAVLAGNTTVISLLLEAGANVDAQNIKGESALDLAKQRKNVWMINHLQEARQAKGYDNPSFLR 283
Cdd:COG0666   209 GADVNAKDNDG-KTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287


                  ..
gi 1327850424 284 KL 285
Cdd:COG0666   288 LL 289
DHHC pfam01529
DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which ...
 428-558 2.49e-40

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: 143.28  E-value: 2.49e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424 428 FCSTCLIRKPVRSKHCGVCNRCIAKFDHHCPWVGNCVGAGNHRYFMGYLFFLLFMICWMIYGCISYWGLHCETTYTKDGF 507
Cdd:pfam01529   7 YCSTCNIYKPPRSKHCRVCNRCVLRFDHHCPWLNNCIGKRNHKYFILFLLYLTLYLILYLVLSLYYLVKLIESSTLFFFL 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1327850424 508 WTYITQiatcspWMFWMFLNSVFHFMWVAVLLMCQMYQIsCLGITTNERMN 558
Cdd:pfam01529  87 ILFLFS------ISIILLILSLFFLLFLGILLFFHLYLI-SRNLTTYEFMK 130
COG5273 COG5273
Uncharacterized protein containing DHHC-type Zn finger [General function prediction only];
348-547 2.29e-33

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


Pssm-ID: 227598 [Multi-domain]  Cd Length: 309  Bit Score: 129.87  E-value: 2.29e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424 348 LPLGIYLATKFWMYVTWFFWFWNDLNFLFIHLPFLANSVALFYnFGKSWKSDPGII--KATEEQKKKTIVELAETGSLDL 425
Cdd:COG5273    30 MFIGLFLLSRIVVYTLLVIVKSLSLVVLFIILFIVILVLASFS-YLLLLVSDPGYLgeNITLSGYRETISRLLDDGKFGT 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424 426 SIFCSTCLIRKPVRSKHCGVCNRCIAKFDHHCPWVGNCVGAGNHRYFMGYLFFLLFMICWMIYGCISY----WGLHCETT 501
Cdd:COG5273   109 ENFCSTCNIYKPPRSHHCSICNRCVLKFDHHCPWINNCVGFRNYRFFYQFLLYTILVALVVLLSTAYYiagiFSIRHDTS 188

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1327850424 502 YTKD-----------GFWTYITqiatcspwMFWMFLNsvfhFMWVAVLLMCQMYQIS 547
Cdd:COG5273   189 LAICflifgcsllgvVFFIITT--------LLLLFLI----YLILNNLTTIEFIQIS 233
Ank_2 pfam12796
Ankyrin repeats (3 copies);
151-245 4.05e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.95  E-value: 4.05e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424 151 IHLAAQFGHTSIVAYLIAKGQDVDMMDQNGMTPLMWAAYRTHsVDPTRLLLTFnvsVNLGDKYHKNTALHWAVLAGNTTV 230
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGH-LEIVKLLLEH---ADVNLKDNGRTALHYAARSGHLEI 76

                          90
                  ....*....|....*
gi 1327850424 231 ISLLLEAGANVDAQN 245
Cdd:pfam12796  77 VKLLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
100-267 2.14e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 91.94  E-value: 2.14e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424 100 ISKGAIVDQLGGDLNSTPLHWATRQGHLSMVVQLMKYGADPSLIDGEGCSCIHLAAQFGHTSIVAYLIAKGQDVDMMDQN 179
Cdd:COG0666     7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424 180 GMTPLMWAAYRTHsVDPTRLLLTFNVSVNLGDKYhKNTALHWAVLAGNTTVISLLLEAGANVDAQNIKGESALDLAKQRK 259
Cdd:COG0666    87 GNTLLHAAARNGD-LEIVKLLLEAGADVNARDKD-GETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANG 164


                  ....*...
gi 1327850424 260 NVWMINHL 267
Cdd:COG0666   165 NLEIVKLL 172
Ank_2 pfam12796
Ankyrin repeats (3 copies);
118-211 4.28e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.39  E-value: 4.28e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424 118 LHWATRQGHLSMVVQLMKYGADPSLIDGEGCSCIHLAAQFGHTSIVAYLIAKGqDVDMMDqNGMTPLMWAAYRTHsVDPT 197
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKD-NGRTALHYAARSGH-LEIV 77

                          90
                  ....*....|....
gi 1327850424 198 RLLLTFNVSVNLGD 211
Cdd:pfam12796  78 KLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
84-177 5.44e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 76.31  E-value: 5.44e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424  84 LHWAAINNRIDLVKYYISKGAIVDQLGGDlNSTPLHWATRQGHLSMVVQLMKYGAdpSLIDGEGCSCIHLAAQFGHTSIV 163
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKN-GRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIV 77

                          90
                  ....*....|....
gi 1327850424 164 AYLIAKGQDVDMMD 177
Cdd:pfam12796  78 KLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
54-144 5.99e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 76.31  E-value: 5.99e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424  54 ATQYGIYERCRELVEAGYDVRQPDKENVTLLHWAAINNRIDLVKYYISKGAIVDQLGGDlnsTPLHWATRQGHLSMVVQL 133
Cdd:pfam12796   4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR---TALHYAARSGHLEIVKLL 80

                          90
                  ....*....|.
gi 1327850424 134 MKYGADPSLID 144
Cdd:pfam12796  81 LEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 42-267 3.24e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 81.25  E-value: 3.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424  42 HIDDYSTWDIVKATQYGIYERCRELVEA----GYDVRQPDKENVTLLHWAA-----INNRIDLVKYYISKGAIVDQlGGD 112
Cdd:PHA03100   26 DLNDYSYKKPVLPLYLAKEARNIDVVKIlldnGADINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLEYGANVNA-PDN 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424 113 LNSTPLHWA--TRQGHLSMVVQLMKYGADPSLIDGEGCSCIHLAAQFGH--TSIVAYLIAKGQDVDMMDqngmtplmwaa 188
Cdd:PHA03100  105 NGITPLLYAisKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKN----------- 173

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1327850424 189 yrthSVDptrLLLTFNVSVNLGDKYHkNTALHWAVLAGNTTVISLLLEAGANVDAQNIKGESALDLAKQRKNVWMINHL 267
Cdd:PHA03100  174 ----RVN---YLLSYGVPINIKDVYG-FTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLL 244
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 61-255 1.31e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 79.62  E-value: 1.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424  61 ERCRELVEAGYDVRQPDKENVTLLHWAAINNRIDLVKYYISKGAIVDqLGGDLNSTPLHWATRQGHLSMVVQLMKYGADP 140
Cdd:PHA02874  105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVN-IEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYA 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424 141 SLIDGEGCSCIHLAAQFGHTSIVAYLIAKGQDVDMMDQNGMTPLMWAAYRTHSVDPtrlLLTFNVSVNLGDkYHKNTALH 220
Cdd:PHA02874  184 NVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIE---LLINNASINDQD-IDGSTPLH 259

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1327850424 221 WAV-LAGNTTVISLLLEAGANVDAQNIKGESALDLA 255
Cdd:PHA02874  260 HAInPPCDIDIIDILLYHKADISIKDNKGENPIDTA 295
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 44-263 6.49e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 75.10  E-value: 6.49e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424  44 DDYSTWDIVKATQYGIYERCRELVEAGYDVRQPDKENVTLLHWAAINNRIDLVKYYISKGAIVDQ--------------- 108
Cdd:PHA02876  175 DIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKndlsllkairnedle 254

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424 109 -------LGGDLNS------TPLHWATRQGHLS-MVVQLMKYGADPSLIDGEGCSCIHLAAQFGH-TSIVAYLIAKGQDV 173
Cdd:PHA02876  255 tslllydAGFSVNSiddcknTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADV 334

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424 174 DMMDQNGMTPLMWAAYRTHSVDPTRLLLTFNVSVNLGDKYHKnTALHWAVLAGNTTVISLLLEAGANVDAQNIKGESALD 253
Cdd:PHA02876  335 NAADRLYITPLHQASTLDRNKDIVITLLELGANVNARDYCDK-TPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALH 413

                         250
                  ....*....|
gi 1327850424 254 LAKQRKNVWM 263
Cdd:PHA02876  414 FALCGTNPYM 423
PHA03095 PHA03095
ankyrin-like protein; Provisional
 66-265 5.47e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 71.59  E-value: 5.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424  66 LVEAGYDVRQPDKENVTLLHWAAINNRID--LVKYYISKGAIVdqlgGDLNS---TPLHWATRQGHLSM-VVQLM-KYGA 138
Cdd:PHA03095  103 LIKAGADVNAKDKVGRTPLHVYLSGFNINpkVIRLLLRKGADV----NALDLygmTPLAVLLKSRNANVeLLRLLiDAGA 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424 139 DPSLIDGEGCSCIHLAAQFGHTS--IVAYLIAKGQDVDMMDQNGMTPLMWAAyrTHSVDPTRLLLTF---NVSVNLGDKY 213
Cdd:PHA03095  179 DVYAVDDRFRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMA--TGSSCKRSLVLPLliaGISINARNRY 256

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1327850424 214 HKnTALHWAVLAGNTTVISLLLEAGANVDAQNIKGESALDLAKQRKNVWMIN 265
Cdd:PHA03095  257 GQ-TPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVR 307
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 94-258 5.83e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 71.45  E-value: 5.83e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424  94 DLVKYYISKGAIVDQLGGDLNSTPLHWATRQGHLSMVVQLMKYGADPSLIDGEGCSCIHLAAQFGHTSIVAYLIAKGQDV 173
Cdd:PHA02878  148 EITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAST 227

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424 174 DMMDQNGMTPLMWAAYRTHSVDPTRLLLTFNVSVNLGDKYHKNTALHWAVlaGNTTVISLLLEAGANVDAQNIKGESALD 253
Cdd:PHA02878  228 DARDKCGNTPLHISVGYCKDYDILKLLLEHGVDVNAKSYILGLTALHSSI--KSERKLKLLLEYGADINSLNSYKLTPLS 305


                  ....*.
gi 1327850424 254 LA-KQR 258
Cdd:PHA02878  306 SAvKQY 311
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 43-255 3.06e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 66.24  E-value: 3.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424  43 IDDYSTWDIVKATQYGIYER-CRELVEAGYDVRQPDKENVTLLHWAAINN-RIDLVKYYISKGAIVDQlGGDLNSTPLHW 120
Cdd:PHA02876  269 IDDCKNTPLHHASQAPSLSRlVPKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNA-ADRLYITPLHQ 347

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424 121 A-TRQGHLSMVVQLMKYGADPSLIDGEGCSCIHLAAQFGHTSIVAYLIAKGQDVDMMDQNGMTPLMWAAYRTHSVDPTRL 199
Cdd:PHA02876  348 AsTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMSVKT 427

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1327850424 200 LLTFNVSVNLGDKYhKNTALHWAVLAG-NTTVISLLLEAGANVDAQNIKGESALDLA 255
Cdd:PHA02876  428 LIDRGANVNSKNKD-LSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIA 483
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 72-240 3.31e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 65.40  E-value: 3.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424  72 DVRQPDKEnvTLLHWAAINNRIDLVKYYISKGAIVDQLGGDLNSTPLHWATRQGHLSMVVQLMKYGADPSLIDGEGCSCI 151
Cdd:PHA02875   62 DVKYPDIE--SELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPL 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424 152 HLAAQFGHTSIVAYLIAKGQDVDMMDQNGMTPLMWA-AYRTHSVdpTRLLLTFNVSVNLGDKYHKNTALHWAVLAGNTTV 230
Cdd:PHA02875  140 HLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAmAKGDIAI--CKMLLDSGANIDYFGKNGCVAALCYAIENNKIDI 217

                         170
                  ....*....|
gi 1327850424 231 ISLLLEAGAN 240
Cdd:PHA02875  218 VRLFIKRGAD 227
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 89-257 9.18e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 64.21  E-value: 9.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424  89 INNriDLVKYYISKGAIVDQLGGDLNsTPLHWATRQGHLSMVVQLMKYGADPSLIDGEGCSCIHLAAQFGHTSIVAYLIA 168
Cdd:PHA02874  102 IEK--DMIKTILDCGIDVNIKDAELK-TFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLE 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424 169 KGQDVDMMDQNGMTPLMWAA----YRThsvdpTRLLLTF--NVSVNLGDKYhknTALHWAVLAgNTTVISLLLEaGANVD 242
Cdd:PHA02874  179 KGAYANVKDNNGESPLHNAAeygdYAC-----IKLLIDHgnHIMNKCKNGF---TPLHNAIIH-NRSAIELLIN-NASIN 248

                         170
                  ....*....|....*
gi 1327850424 243 AQNIKGESALDLAKQ 257
Cdd:PHA02874  249 DQDIDGSTPLHHAIN 263
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 123-254 1.16e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 64.70  E-value: 1.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424 123 RQGHLSMVVQLMKYGADPSLIDGEGCSCIHLAAQFGHTSIVAYLIAKGQDVDMMDQNGMTPLMWA--------------- 187
Cdd:PHA02876  154 QQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAvdsknidtikaiidn 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424 188 -------------AYRTHSVDPTRLLLTFNVSVNLGDKYhKNTALHWAVLAGN-TTVISLLLEAGANVDAQNIKGESALD 253
Cdd:PHA02876  234 rsninkndlsllkAIRNEDLETSLLLYDAGFSVNSIDDC-KNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLY 312


                  .
gi 1327850424 254 L 254
Cdd:PHA02876  313 L 313
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 78-304 1.74e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 63.47  E-value: 1.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424  78 KENVTLLHWAAINNRIDLVKYYISKGAIVDQLGGDlNSTPLHWATRQGHLSMVVQLMKYGADPSLIDGEGCSCIHLAAQF 157
Cdd:PHA02875  100 KDGMTPLHLATILKKLDIMKLLIARGADPDIPNTD-KFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAK 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424 158 GHTSIVAYLIAKGQDVDMMDQNGMTPLMWAAYRTHSVDPTRLLLT----------------------FNVSVNLGD---- 211
Cdd:PHA02875  179 GDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIKrgadcnimfmiegeectildmiCNMCTNLESeaid 258

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424 212 --------KYHKNTALHWAVLAGNTTVI---SLLLEAGAN-------VDAQNIKGESALDLAKQRKNVWMINHLQEARQA 273
Cdd:PHA02875  259 aliadiaiRIHKKTIRRDEGFKNNMSTIedkEEFKDVFEKciielrrIKSEKIGKKNILDLCILEKNSHNLDENILARHS 338

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1327850424 274 KG----YDNPSFLRKL---KADKEFRQKVMLGTPFLVI 304
Cdd:PHA02875  339 KKilglNDEAHFYKYLlkeAADIALKRAEAIESAIRVI 376
PHA03095 PHA03095
ankyrin-like protein; Provisional
 64-285 4.12e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 62.35  E-value: 4.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424  64 RELVEAGYDVRQPDKENVTLLHWAAIN-NRIDLVKYYISKGAIVDQlGGDLNSTPLHwatrqghlsmvvqlmkygadpsl 142
Cdd:PHA03095   67 RLLLEAGADVNAPERCGFTPLHLYLYNaTTLDVIKLLIKAGADVNA-KDKVGRTPLH----------------------- 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424 143 idgegcscIHLAAQFGHTSIVAYLIAKGQDVDMMDQNGMTPLmwAAY-RTHSVDPT--RLLL-----TFNVSVNL----- 209
Cdd:PHA03095  123 --------VYLSGFNINPKVIRLLLRKGADVNALDLYGMTPL--AVLlKSRNANVEllRLLIdagadVYAVDDRFrsllh 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424 210 ------------------------GDKYHKNTALHWAVLAGN--TTVISLLLEAGANVDAQNIKGESALdlakqrknvwm 263
Cdd:PHA03095  193 hhlqsfkprarivreliragcdpaATDMLGNTPLHSMATGSSckRSLVLPLLIAGISINARNRYGQTPL----------- 261

                         250       260
                  ....*....|....*....|..
gi 1327850424 264 inHLqearqAKGYDNPSFLRKL 285
Cdd:PHA03095  262 --HY-----AAVFNNPRACRRL 276
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 53-179 8.52e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 61.22  E-value: 8.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424  53 KATQYGIYErcrELVEAGYDVRQPDKENVTLLHWAAINNRIDL--VKYYISKGAIVDQ---------LGGDLNS------ 115
Cdd:PHA03100  117 KSNSYSIVE---YLLDNGANVNIKNSDGENLLHLYLESNKIDLkiLKLLIDKGVDINAknrvnyllsYGVPINIkdvygf 193

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1327850424 116 TPLHWATRQGHLSMVVQLMKYGADPSLIDGEGCSCIHLAAQFGHTSIVAYLIAKGQDVDMMDQN 179
Cdd:PHA03100  194 TPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 93-252 2.92e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 59.62  E-value: 2.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424  93 IDLVKYYISKGAIVDQLGGDLNStPLHWATRQGHLSMVVQLM---KYGADpsLIDGEGCSCIHLAAQFGHTSIVAYLIAK 169
Cdd:PHA02875   48 SEAIKLLMKHGAIPDVKYPDIES-ELHDAVEEGDVKAVEELLdlgKFADD--VFYKDGMTPLHLATILKKLDIMKLLIAR 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424 170 GQDVDMMDQNGMTPLMWAAYrTHSVDPTRLLLTFNVSVNLGDKYhKNTALHWAVLAGNTTVISLLLEAGANVDAQNIKGE 249
Cdd:PHA02875  125 GADPDIPNTDKFSPLHLAVM-MGDIKGIELLIDHKACLDIEDCC-GCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGC 202


                  ...
gi 1327850424 250 SAL 252
Cdd:PHA02875  203 VAA 205
Ank_4 pfam13637
Ankyrin repeats (many copies);
114-167 4.76e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.66  E-value: 4.76e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1327850424 114 NSTPLHWATRQGHLSMVVQLMKYGADPSLIDGEGCSCIHLAAQFGHTSIVAYLI 167
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 125-297 1.51e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 57.96  E-value: 1.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424 125 GHLSMVVQLMKYGADPSLIDGEGCSCIHLAAQFGHTSIVAYLIAKGQDVDMMDQNGMTPlMWAAYRTHSVDPTRLLLTFn 204
Cdd:PLN03192  536 GNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTA-LWNAISAKHHKIFRILYHF- 613

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424 205 vsVNLGDKYHKNTALHWAVLAGNTTVISLLLEAGANVDAQNIKGESALDLAKQRKNVWMINHL----QEARQAKGYDN-- 278
Cdd:PLN03192  614 --ASISDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLimngADVDKANTDDDfs 691

                         170
                  ....*....|....*....
gi 1327850424 279 PSFLRKLKADKEFRQKVML 297
Cdd:PLN03192  692 PTELRELLQKRELGHSITI 710
PHA03095 PHA03095
ankyrin-like protein; Provisional
 64-184 8.21e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 55.03  E-value: 8.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424  64 RELVEAGYDVRQPDKENVTLLHWAAINNRID--LVKYYISKGaiVDQLGGD-LNSTPLHWATRQGHL--SMVVQLMKYGA 138
Cdd:PHA03095  171 RLLIDAGADVYAVDDRFRSLLHHHLQSFKPRarIVRELIRAG--CDPAATDmLGNTPLHSMATGSSCkrSLVLPLLIAGI 248

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1327850424 139 DPSLIDGEGCSCIHLAAQFGHTSIVAYLIAKGQDVDMMDQNGMTPL 184
Cdd:PHA03095  249 SINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 116-261 9.62e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 54.61  E-value: 9.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424 116 TPLHWATRQGHLSMVVQLMKYGADPSLIDGEGCSCIHLAAQFGHTSIVAYLIAKGQDV-DMMDQNGMTPLmWAAYRTHSV 194
Cdd:PHA02875   37 SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAdDVFYKDGMTPL-HLATILKKL 115

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1327850424 195 DPTRLLLTFNVSVNLGDKyHKNTALHWAVLAGNTTVISLLLEAGANVDAQNIKGESALDLAKQRKNV 261
Cdd:PHA02875  116 DIMKLLIARGADPDIPNT-DKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDI 181
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 64-255 1.33e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 54.50  E-value: 1.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424  64 RELVEAGYDVRQPDKENVTLLHWAAINNRIDLVKYYISKgAIVDQLGGDLNSTPLHWATRQGHLSMVVQLMKYGADPSLI 143
Cdd:PHA02878   54 KSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRS-INKCSVFYTLVAIKDAFNNRNVEIFKIILTNRYKNIQTID 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424 144 DGEGCSCIHlaAQFGHTSIVAYLIAKGQDVDMMDQN-GMTPLMWAAyRTHSVDPTRLLLTFNVSVNLGDKYHkNTALHWA 222
Cdd:PHA02878  133 LVYIDKKSK--DDIIEAEITKLLLSYGADINMKDRHkGNTALHYAT-ENKDQRLTELLLSYGANVNIPDKTN-NSPLHHA 208

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1327850424 223 VLAGNTTVISLLLEAGANVDAQNIKGESALDLA 255
Cdd:PHA02878  209 VKHYNKPIVHILLENGASTDARDKCGNTPLHIS 241
Ank_5 pfam13857
Ankyrin repeats (many copies);
199-255 1.51e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.50  E-value: 1.51e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1327850424 199 LLLTFNVSVNLGDKyHKNTALHWAVLAGNTTVISLLLEAGANVDAQNIKGESALDLA 255
Cdd:pfam13857   1 LLEHGPIDLNRLDG-EGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
149-192 2.54e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.65  E-value: 2.54e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1327850424 149 SCIHLAAQFGHTSIVAYLIAKGQDVDMMDQNGMTPLMWAAYRTH 192
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGN 46
Ank_4 pfam13637
Ankyrin repeats (many copies);
80-130 2.80e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.65  E-value: 2.80e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1327850424  80 NVTLLHWAAINNRIDLVKYYISKGAIVDQLGGDLNsTPLHWATRQGHLSMV 130
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGE-TALHFAASNGNVEVL 50
PHA03095 PHA03095
ankyrin-like protein; Provisional
 64-177 2.14e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 50.41  E-value: 2.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424  64 RELVEAGYDVRQPDKENVTLLHWAAINN--RIDLVKYYISKGAIVDQLGgDLNSTPLHWATRQGHLSMVVQLMKYGADPS 141
Cdd:PHA03095  206 RELIRAGCDPAATDMLGNTPLHSMATGSscKRSLVLPLLIAGISINARN-RYGQTPLHYAAVFNNPRACRRLIALGADIN 284

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1327850424 142 LIDGEGCSCIHLAAQFGHTSIVAYLIAKGQDVDMMD 177
Cdd:PHA03095  285 AVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVA 320
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 110-180 7.17e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.13  E-value: 7.17e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1327850424 110 GGDLNS------TPLHWATRQGHLSMVVQLMKYGADPSLIDGEGCSCIHLAAQFGHTSIVAYLIAKGQDVDMMDQNG 180
Cdd:PTZ00322  105 GADPNCrdydgrTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGANA 181
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 214-245 8.60e-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: 42.66  E-value: 8.60e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1327850424 214 HKNTALHWAVL-AGNTTVISLLLEAGANVDAQN 245
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
Ank_4 pfam13637
Ankyrin repeats (many copies);
216-255 2.88e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.88  E-value: 2.88e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1327850424 216 NTALHWAVLAGNTTVISLLLEAGANVDAQNIKGESALDLA 255
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFA 41
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 112-269 3.26e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 46.88  E-value: 3.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424 112 DLNSTPLHWATRQGHLSMVVQLMKYGADPSLIDGEGCSCIHLAAQFGHTSIVAYLIAKGQDVDMMDqngmTPLMwaayrt 191
Cdd:PHA02874   33 DETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSILP----IPCI------ 102

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1327850424 192 hSVDPTRLLLTFNVSVNLGDKYHKnTALHWAVLAGNTTVISLLLEAGANVDAQNIKGESALDLAKQRKNVWMINHLQE 269
Cdd:PHA02874  103 -EKDMIKTILDCGIDVNIKDAELK-TFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLE 178
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 133-184 8.66e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 45.66  E-value: 8.66e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1327850424 133 LMKYGADPSLIDGEGCSCIHLAAQFGHTSIVAYLIAKGQDVDMMDQNGMTPL 184
Cdd:PTZ00322  101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPL 152
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 116-246 1.33e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 45.24  E-value: 1.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424 116 TPLHWATRQGHLSMVVQLMKYGADPSLIDGEGCSCIHLAAQFGHTSI--VAYLIAKGQDvdmmDQNGMTPLMWAAYRtHS 193
Cdd:PLN03192  560 TPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIfrILYHFASISD----PHAAGDLLCTAAKR-ND 634

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1327850424 194 VDPTRLLLTFNVSVNLGDkYHKNTALHWAVLAGNTTVISLLLEAGANVDAQNI 246
Cdd:PLN03192  635 LTAMKELLKQGLNVDSED-HQGATALQVAMAEDHVDMVRLLIMNGADVDKANT 686
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 214-243 1.75e-04

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: 39.11  E-value: 1.75e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1327850424  214 HKNTALHWAVLAGNTTVISLLLEAGANVDA 243
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_2 pfam12796
Ankyrin repeats (3 copies);
219-276 2.45e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 40.48  E-value: 2.45e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1327850424 219 LHWAVLAGNTTVISLLLEAGANVDAQNIKGESALDLAKQRKNV----WMINHLQEARQAKGY 276
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLeivkLLLEHADVNLKDNGR 62
Ank_5 pfam13857
Ankyrin repeats (many copies);
99-154 2.48e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.25  E-value: 2.48e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1327850424  99 YISKGAIVDQLGGDLNSTPLHWATRQGHLSMVVQLMKYGADPSLIDGEGCSCIHLA 154
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 198-257 2.53e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.12  E-value: 2.53e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424 198 RLLLTFNVSVNLGDkYHKNTALHWAVLAGNTTVISLLLEAGANVDAQNIKGESALDLAKQ 257
Cdd:PTZ00322   99 RILLTGGADPNCRD-YDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEE 157
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 84-260 2.76e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 43.72  E-value: 2.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424  84 LHWAAINNRIDLVKYYISKGAIVDQLGGDlNSTPLHWATRQGHLsmvvQLMKYGADPSLIDGEGCSCIHLAAQFGHTSIV 163
Cdd:PHA02878   41 LHQAVEARNLDVVKSLLTRGHNVNQPDHR-DLTPLHIICKEPNK----LGMKEMIRSINKCSVFYTLVAIKDAFNNRNVE 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424 164 aylIAKGQDVDMMDQNGMTPLMWaaYRTHSVDP------TRLLLTFNVSVNLGDKYHKNTALHWAVLAGNTTVISLLLEA 237
Cdd:PHA02878  116 ---IFKIILTNRYKNIQTIDLVY--IDKKSKDDiieaeiTKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSY 190

                         170       180
                  ....*....|....*....|...
gi 1327850424 238 GANVDAQNIKGESALDLAKQRKN 260
Cdd:PHA02878  191 GANVNIPDKTNNSPLHHAVKHYN 213
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 60-184 3.65e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 43.70  E-value: 3.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424  60 YERC-RELVEAGYDVRQPDKENVTLLhWAAI---NNRIDLVKYYISkgAIVD-QLGGDLnstpLHWATRQGHLSMVVQLM 134
Cdd:PLN03192  570 YEDCvLVLLKHACNVHIRDANGNTAL-WNAIsakHHKIFRILYHFA--SISDpHAAGDL----LCTAAKRNDLTAMKELL 642

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1327850424 135 KYGADPSLIDGEGCSCIHLAAQFGHTSIVAYLIAKGQDVDMMD-QNGMTPL 184
Cdd:PLN03192  643 KQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANtDDDFSPT 693
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 116-144 6.54e-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: 6.54e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1327850424 116 TPLHWA-TRQGHLSMVVQLMKYGADPSLID 144
Cdd:pfam00023   4 TPLHLAaGRRGNLEIVKLLLSKGADVNARD 33
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 125-271 6.61e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 42.67  E-value: 6.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424 125 GHLSMVVQLMKYGADPSLIDGEGCSCIHLAAQFGHTSIVAYLIAKGQDVDMMDQNGMTPLMWAAYRThSVDPTRLLLTFN 204
Cdd:PHA02875   13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEG-DVKAVEELLDLG 91

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1327850424 205 VSVNlgDKYHK--NTALHWAVLAGNTTVISLLLEAGANVDAQNIKGESALDLAKQRKNVWMINHLQEAR 271
Cdd:PHA02875   92 KFAD--DVFYKdgMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHK 158
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 214-243 7.42e-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: 37.24  E-value: 7.42e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1327850424 214 HKNTALHWAVLAGNTTVISLLLEAGANVDA 243
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 112-259 8.71e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 40.96  E-value: 8.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424 112 DLNSTPLHWATRQGHLS--MVVQLMKYGADPS-LIDGEGCSCIHLAAQFGHT---SIVAYLIAKGQDVDMMDQNGMTPL- 184
Cdd:PHA02859   49 DLYETPIFSCLEKDKVNveILKFLIENGADVNfKTRDNNLSALHHYLSFNKNvepEILKILIDSGSSITEEDEDGKNLLh 128

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1327850424 185 MWAAYRTHSVDPTRLLLTFNVSVNLGDKYHKNTALHWAVLAGNTTVISLLLEAGANVDAQNIKGESALDLAKQRK 259
Cdd:PHA02859  129 MYMCNFNVRINVIKLLIDSGVSFLNKDFDNNNILYSYILFHSDKKIFDFLTSLGIDINETNKSGYNCYDLIKFRN 203
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 146-177 9.59e-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: 36.88  E-value: 9.59e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1327850424 146 EGCSCIHLAA-QFGHTSIVAYLIAKGQDVDMMD 177
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 199-286 1.12e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 41.97  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424 199 LLLTFNVSVNLGDKYHKnTALHWAVLAGNTTVISLLLEAGANVDAQNIKGESALDLAKQRKNVWMINHLQEARQAKGYDN 278
Cdd:PHA02876  163 MLLEGGADVNAKDIYCI-TPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKND 241


                  ....*...
gi 1327850424 279 PSFLRKLK 286
Cdd:PHA02876  242 LSLLKAIR 249
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 116-142 1.13e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.80  E-value: 1.13e-03
                           10        20
                   ....*....|....*....|....*..
gi 1327850424  116 TPLHWATRQGHLSMVVQLMKYGADPSL 142
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 179-212 1.16e-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. 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: 36.88  E-value: 1.16e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1327850424 179 NGMTPLMWAAYRTHSVDPTRLLLTFNVSVNLGDK 212
Cdd:pfam00023   1 DGNTPLHLAAGRRGNLEIVKLLLSKGADVNARDK 34
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 82-271 1.37e-03

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 41.54  E-value: 1.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424  82 TLLHWAAINNRIDLVKYYI--SKGAIVDQLGGDL--NSTPLHWATRQGHLSMVVQLMKYGADPS--------LIDGEGCS 149
Cdd:cd22192    53 TALHVAALYDNLEAAVVLMeaAPELVNEPMTSDLyqGETALHIAVVNQNLNLVRELIARGADVVspratgtfFRPGPKNL 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424 150 C------IHLAAQFGHTSIVAYLIAKGQDVDMMDQNGmtplmwaayrthsvdptrllltfnvsvnlgdkyhkNTALHWAV 223
Cdd:cd22192   133 IyygehpLSFAACVGNEEIVRLLIEHGADIRAQDSLG-----------------------------------NTVLHILV 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1327850424 224 LAGNTT----VISLLLEAGANVDAQ------NIKGESALDLAKQRKNVWMINHLQEAR 271
Cdd:cd22192   178 LQPNKTfacqMYDLILSYDKEDDLQpldlvpNNQGLTPFKLAAKEGNIVMFQHLVQKR 235
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 82-107 1.39e-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: 36.47  E-value: 1.39e-03
                          10        20
                  ....*....|....*....|....*.
gi 1327850424  82 TLLHWAAINNRIDLVKYYISKGAIVD 107
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADIN 29
Ank_5 pfam13857
Ankyrin repeats (many copies);
138-184 1.42e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.94  E-value: 1.42e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1327850424 138 ADPSLIDGEGCSCIHLAAQFGHTSIVAYLIAKGQDVDMMDQNGMTPL 184
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 146-175 3.86e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.26  E-value: 3.86e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1327850424  146 EGCSCIHLAAQFGHTSIVAYLIAKGQDVDM 175
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 54-178 5.69e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 39.56  E-value: 5.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850424  54 ATQYGIYERCRELVEAGYDVRQPDKENVTLLHWAAINNRiDLVKYYISKGAIVDQlggDLN-STPLHWATRQGHLSMVVQ 132
Cdd:PHA02874  197 AAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLINNASINDQ---DIDgSTPLHHAINPPCDIDIID 272

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1327850424 133 LMKY-GADPSLIDGEGCSCIHLAAQF-GHTSIVAYLIAKGQDVDMMDQ 178
Cdd:PHA02874  273 ILLYhKADISIKDNKGENPIDTAFKYiNKDPVIKDIIANAVLIKEADK 320
Ank_5 pfam13857
Ankyrin repeats (many copies);
166-222 7.80e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.01  E-value: 7.80e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1327850424 166 LIAKGQ-DVDMMDQNGMTPLMWAAYRtHSVDPTRLLLTFNVSVNLGDKyHKNTALHWA 222
Cdd:pfam13857   1 LLEHGPiDLNRLDGEGYTPLHVAAKY-GALEIVRVLLAYGVDLNLKDE-EGLTALDLA 56
 
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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