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Conserved domains on  [gi|103471993|ref|NP_056151|]
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palmitoyltransferase ZDHHC17 isoform 1 [Homo sapiens]

Protein Classification

DHHC family palmitoyltransferase( 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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
52-307 9.85e-46

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 163.97  E-value: 9.85e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993  52 HIDDYSTWDIVKATQYGIYERCRELVEAGYDVRQPDKENVTLLHWAAINNRIDLVKYYISKGAIVDQLGGDLNsTPLHWA 131
Cdd:COG0666   16 LLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGN-TLLHAA 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993 132 TRQGHLSMVVQLMKYGADPSLIDGEGCSCIHLAAQFGHTSIVAYLIAKGQDVDMMDQNGMTPLMWAAYRTHsVDPTRLLL 211
Cdd:COG0666   95 ARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN-LEIVKLLL 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993 212 TFNVSVNLGDKYhKNTALHWAVLAGNTTVISLLLEAGANVDAQNIKGESALDLAKQRKNVWMINHLQEARQAKGYDNPSF 291
Cdd:COG0666  174 EAGADVNARDND-GETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDG 252

                        250
                 ....*....|....*.
gi 103471993 292 LRKLKADKEFRQKVML 307
Cdd:COG0666  253 LTALLLAAAAGAALIV 268
DHHC pfam01529
DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which ...
 438-568 1.64e-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: 144.05  E-value: 1.64e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993  438 FCSTCLIRKPVRSKHCGVCNRCIAKFDHHCPWVGNCVGAGNHRYFMGYLFFLLFMICWMIYGCISYWGLHCETTYTKDGF 517
Cdd:pfam01529   7 YCSTCNIYKPPRSKHCRVCNRCVLRFDHHCPWLNNCIGKRNHKYFILFLLYLTLYLILYLVLSLYYLVKLIESSTLFFFL 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 103471993  518 WTYITQiatcspWMFWMFLNSVFHFMWVAVLLMCQMYQIsCLGITTNERMN 568
Cdd:pfam01529  87 ILFLFS------ISIILLILSLFFLLFLGILLFFHLYLI-SRNLTTYEFMK 130
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
52-307 9.85e-46

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 163.97  E-value: 9.85e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993  52 HIDDYSTWDIVKATQYGIYERCRELVEAGYDVRQPDKENVTLLHWAAINNRIDLVKYYISKGAIVDQLGGDLNsTPLHWA 131
Cdd:COG0666   16 LLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGN-TLLHAA 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993 132 TRQGHLSMVVQLMKYGADPSLIDGEGCSCIHLAAQFGHTSIVAYLIAKGQDVDMMDQNGMTPLMWAAYRTHsVDPTRLLL 211
Cdd:COG0666   95 ARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN-LEIVKLLL 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993 212 TFNVSVNLGDKYhKNTALHWAVLAGNTTVISLLLEAGANVDAQNIKGESALDLAKQRKNVWMINHLQEARQAKGYDNPSF 291
Cdd:COG0666  174 EAGADVNARDND-GETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDG 252

                        250
                 ....*....|....*.
gi 103471993 292 LRKLKADKEFRQKVML 307
Cdd:COG0666  253 LTALLLAAAAGAALIV 268
DHHC pfam01529
DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which ...
 438-568 1.64e-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: 144.05  E-value: 1.64e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993  438 FCSTCLIRKPVRSKHCGVCNRCIAKFDHHCPWVGNCVGAGNHRYFMGYLFFLLFMICWMIYGCISYWGLHCETTYTKDGF 517
Cdd:pfam01529   7 YCSTCNIYKPPRSKHCRVCNRCVLRFDHHCPWLNNCIGKRNHKYFILFLLYLTLYLILYLVLSLYYLVKLIESSTLFFFL 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 103471993  518 WTYITQiatcspWMFWMFLNSVFHFMWVAVLLMCQMYQIsCLGITTNERMN 568
Cdd:pfam01529  87 ILFLFS------ISIILLILSLFFLLFLGILLFFHLYLI-SRNLTTYEFMK 130
COG5273 COG5273
Uncharacterized protein containing DHHC-type Zn finger [General function prediction only];
358-557 1.53e-33

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


Pssm-ID: 227598 [Multi-domain]  Cd Length: 309  Bit Score: 130.64  E-value: 1.53e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993 358 LPLGIYLATKFWMYVTWFFWFWNDLNFLFIHLPFLANSVALFYnFGKSWKSDPGII--KATEEQKKKTIVELAETGSLDL 435
Cdd:COG5273   30 MFIGLFLLSRIVVYTLLVIVKSLSLVVLFIILFIVILVLASFS-YLLLLVSDPGYLgeNITLSGYRETISRLLDDGKFGT 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993 436 SIFCSTCLIRKPVRSKHCGVCNRCIAKFDHHCPWVGNCVGAGNHRYFMGYLFFLLFMICWMIYGCISY----WGLHCETT 511
Cdd:COG5273  109 ENFCSTCNIYKPPRSHHCSICNRCVLKFDHHCPWINNCVGFRNYRFFYQFLLYTILVALVVLLSTAYYiagiFSIRHDTS 188

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 103471993 512 YTKD-----------GFWTYITqiatcspwMFWMFLNsvfhFMWVAVLLMCQMYQIS 557
Cdd:COG5273  189 LAICflifgcsllgvVFFIITT--------LLLLFLI----YLILNNLTTIEFIQIS 233
Ank_2 pfam12796
Ankyrin repeats (3 copies);
161-255 3.30e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 91.33  E-value: 3.30e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993  161 IHLAAQFGHTSIVAYLIAKGQDVDMMDQNGMTPLMWAAYRTHsVDPTRLLLTFnvsVNLGDKYHKNTALHWAVLAGNTTV 240
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGH-LEIVKLLLEH---ADVNLKDNGRTALHYAARSGHLEI 76

                          90
                  ....*....|....*
gi 103471993  241 ISLLLEAGANVDAQN 255
Cdd:pfam12796  77 VKLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 52-277 2.83e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 81.25  E-value: 2.83e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993  52 HIDDYSTWDIVKATQYGIYERCRELVEA----GYDVRQPDKENVTLLHWAA-----INNRIDLVKYYISKGAIVDQlGGD 122
Cdd:PHA03100  26 DLNDYSYKKPVLPLYLAKEARNIDVVKIlldnGADINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLEYGANVNA-PDN 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993 123 LNSTPLHWA--TRQGHLSMVVQLMKYGADPSLIDGEGCSCIHLAAQFGH--TSIVAYLIAKGQDVDMMDqngmtplmwaa 198
Cdd:PHA03100 105 NGITPLLYAisKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKN----------- 173

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 103471993 199 yrthSVDptrLLLTFNVSVNLGDKYHkNTALHWAVLAGNTTVISLLLEAGANVDAQNIKGESALDLAKQRKNVWMINHL 277
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 ...
 224-253 1.58e-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: 1.58e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 103471993   224 HKNTALHWAVLAGNTTVISLLLEAGANVDA 253
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 92-281 1.38e-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: 1.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993  92 TLLHWAAINNRIDLVKYYI--SKGAIVDQLGGDL--NSTPLHWATRQGHLSMVVQLMKYGADPS--------LIDGEGCS 159
Cdd:cd22192   53 TALHVAALYDNLEAAVVLMeaAPELVNEPMTSDLyqGETALHIAVVNQNLNLVRELIARGADVVspratgtfFRPGPKNL 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993 160 C------IHLAAQFGHTSIVAYLIAKGQDVDMMDQNGmtplmwaayrthsvdptrllltfnvsvnlgdkyhkNTALHWAV 233
Cdd:cd22192  133 IyygehpLSFAACVGNEEIVRLLIEHGADIRAQDSLG-----------------------------------NTVLHILV 177

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 103471993 234 LAGNTT----VISLLLEAGANVDAQ------NIKGESALDLAKQRKNVWMINHLQEAR 281
Cdd:cd22192  178 LQPNKTfacqMYDLILSYDKEDDLQpldlvpNNQGLTPFKLAAKEGNIVMFQHLVQKR 235
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
52-307 9.85e-46

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 163.97  E-value: 9.85e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993  52 HIDDYSTWDIVKATQYGIYERCRELVEAGYDVRQPDKENVTLLHWAAINNRIDLVKYYISKGAIVDQLGGDLNsTPLHWA 131
Cdd:COG0666   16 LLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGN-TLLHAA 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993 132 TRQGHLSMVVQLMKYGADPSLIDGEGCSCIHLAAQFGHTSIVAYLIAKGQDVDMMDQNGMTPLMWAAYRTHsVDPTRLLL 211
Cdd:COG0666   95 ARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN-LEIVKLLL 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993 212 TFNVSVNLGDKYhKNTALHWAVLAGNTTVISLLLEAGANVDAQNIKGESALDLAKQRKNVWMINHLQEARQAKGYDNPSF 291
Cdd:COG0666  174 EAGADVNARDND-GETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDG 252

                        250
                 ....*....|....*.
gi 103471993 292 LRKLKADKEFRQKVML 307
Cdd:COG0666  253 LTALLLAAAAGAALIV 268
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
54-295 1.18e-44

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 160.89  E-value: 1.18e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993  54 DDYSTWDIVKATQYGIYERCRELVEAGYDVRQPDKENVTLLHWAAINNRIDLVKYYISKGAIVDQLGGDLNsTPLHWATR 133
Cdd:COG0666   51 DALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGE-TPLHLAAY 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993 134 QGHLSMVVQLMKYGADPSLIDGEGCSCIHLAAQFGHTSIVAYLIAKGQDVDMMDQNGMTPLMWAAYRTHsVDPTRLLLTF 213
Cdd:COG0666  130 NGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGH-LEIVKLLLEA 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993 214 NVSVNLGDKYHkNTALHWAVLAGNTTVISLLLEAGANVDAQNIKGESALDLAKQRKNVWMINHLQEARQAKGYDNPSFLR 293
Cdd:COG0666  209 GADVNAKDNDG-KTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287


                 ..
gi 103471993 294 KL 295
Cdd:COG0666  288 LL 289
DHHC pfam01529
DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which ...
 438-568 1.64e-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: 144.05  E-value: 1.64e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993  438 FCSTCLIRKPVRSKHCGVCNRCIAKFDHHCPWVGNCVGAGNHRYFMGYLFFLLFMICWMIYGCISYWGLHCETTYTKDGF 517
Cdd:pfam01529   7 YCSTCNIYKPPRSKHCRVCNRCVLRFDHHCPWLNNCIGKRNHKYFILFLLYLTLYLILYLVLSLYYLVKLIESSTLFFFL 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 103471993  518 WTYITQiatcspWMFWMFLNSVFHFMWVAVLLMCQMYQIsCLGITTNERMN 568
Cdd:pfam01529  87 ILFLFS------ISIILLILSLFFLLFLGILLFFHLYLI-SRNLTTYEFMK 130
COG5273 COG5273
Uncharacterized protein containing DHHC-type Zn finger [General function prediction only];
358-557 1.53e-33

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


Pssm-ID: 227598 [Multi-domain]  Cd Length: 309  Bit Score: 130.64  E-value: 1.53e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993 358 LPLGIYLATKFWMYVTWFFWFWNDLNFLFIHLPFLANSVALFYnFGKSWKSDPGII--KATEEQKKKTIVELAETGSLDL 435
Cdd:COG5273   30 MFIGLFLLSRIVVYTLLVIVKSLSLVVLFIILFIVILVLASFS-YLLLLVSDPGYLgeNITLSGYRETISRLLDDGKFGT 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993 436 SIFCSTCLIRKPVRSKHCGVCNRCIAKFDHHCPWVGNCVGAGNHRYFMGYLFFLLFMICWMIYGCISY----WGLHCETT 511
Cdd:COG5273  109 ENFCSTCNIYKPPRSHHCSICNRCVLKFDHHCPWINNCVGFRNYRFFYQFLLYTILVALVVLLSTAYYiagiFSIRHDTS 188

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 103471993 512 YTKD-----------GFWTYITqiatcspwMFWMFLNsvfhFMWVAVLLMCQMYQIS 557
Cdd:COG5273  189 LAICflifgcsllgvVFFIITT--------LLLLFLI----YLILNNLTTIEFIQIS 233
Ank_2 pfam12796
Ankyrin repeats (3 copies);
161-255 3.30e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 91.33  E-value: 3.30e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993  161 IHLAAQFGHTSIVAYLIAKGQDVDMMDQNGMTPLMWAAYRTHsVDPTRLLLTFnvsVNLGDKYHKNTALHWAVLAGNTTV 240
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGH-LEIVKLLLEH---ADVNLKDNGRTALHYAARSGHLEI 76

                          90
                  ....*....|....*
gi 103471993  241 ISLLLEAGANVDAQN 255
Cdd:pfam12796  77 VKLLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
110-277 2.19e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 91.94  E-value: 2.19e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993 110 ISKGAIVDQLGGDLNSTPLHWATRQGHLSMVVQLMKYGADPSLIDGEGCSCIHLAAQFGHTSIVAYLIAKGQDVDMMDQN 189
Cdd:COG0666    7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993 190 GMTPLMWAAYRTHsVDPTRLLLTFNVSVNLGDKYhKNTALHWAVLAGNTTVISLLLEAGANVDAQNIKGESALDLAKQRK 269
Cdd:COG0666   87 GNTLLHAAARNGD-LEIVKLLLEAGADVNARDKD-GETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANG 164


                 ....*...
gi 103471993 270 NVWMINHL 277
Cdd:COG0666  165 NLEIVKLL 172
Ank_2 pfam12796
Ankyrin repeats (3 copies);
128-221 3.35e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.77  E-value: 3.35e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993  128 LHWATRQGHLSMVVQLMKYGADPSLIDGEGCSCIHLAAQFGHTSIVAYLIAKGqDVDMMDqNGMTPLMWAAYRTHsVDPT 207
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKD-NGRTALHYAARSGH-LEIV 77

                          90
                  ....*....|....
gi 103471993  208 RLLLTFNVSVNLGD 221
Cdd:pfam12796  78 KLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
94-187 4.60e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 76.69  E-value: 4.60e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993   94 LHWAAINNRIDLVKYYISKGAIVDQLGGDlNSTPLHWATRQGHLSMVVQLMKYGAdpSLIDGEGCSCIHLAAQFGHTSIV 173
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKN-GRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIV 77

                          90
                  ....*....|....
gi 103471993  174 AYLIAKGQDVDMMD 187
Cdd:pfam12796  78 KLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
64-154 5.27e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 76.31  E-value: 5.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993   64 ATQYGIYERCRELVEAGYDVRQPDKENVTLLHWAAINNRIDLVKYYISKGAIVDQLGGDlnsTPLHWATRQGHLSMVVQL 143
Cdd:pfam12796   4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR---TALHYAARSGHLEIVKLL 80

                          90
                  ....*....|.
gi 103471993  144 MKYGADPSLID 154
Cdd:pfam12796  81 LEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 52-277 2.83e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 81.25  E-value: 2.83e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993  52 HIDDYSTWDIVKATQYGIYERCRELVEA----GYDVRQPDKENVTLLHWAA-----INNRIDLVKYYISKGAIVDQlGGD 122
Cdd:PHA03100  26 DLNDYSYKKPVLPLYLAKEARNIDVVKIlldnGADINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLEYGANVNA-PDN 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993 123 LNSTPLHWA--TRQGHLSMVVQLMKYGADPSLIDGEGCSCIHLAAQFGH--TSIVAYLIAKGQDVDMMDqngmtplmwaa 198
Cdd:PHA03100 105 NGITPLLYAisKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKN----------- 173

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 103471993 199 yrthSVDptrLLLTFNVSVNLGDKYHkNTALHWAVLAGNTTVISLLLEAGANVDAQNIKGESALDLAKQRKNVWMINHL 277
Cdd:PHA03100 174 ----RVN---YLLSYGVPINIKDVYG-FTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLL 244
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 71-265 1.34e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 79.62  E-value: 1.34e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993  71 ERCRELVEAGYDVRQPDKENVTLLHWAAINNRIDLVKYYISKGAIVDqLGGDLNSTPLHWATRQGHLSMVVQLMKYGADP 150
Cdd:PHA02874 105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVN-IEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYA 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993 151 SLIDGEGCSCIHLAAQFGHTSIVAYLIAKGQDVDMMDQNGMTPLMWAAYRTHSVDPtrlLLTFNVSVNLGDkYHKNTALH 230
Cdd:PHA02874 184 NVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIE---LLINNASINDQD-IDGSTPLH 259

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 103471993 231 WAV-LAGNTTVISLLLEAGANVDAQNIKGESALDLA 265
Cdd:PHA02874 260 HAInPPCDIDIIDILLYHKADISIKDNKGENPIDTA 295
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 54-273 6.69e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 75.10  E-value: 6.69e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993  54 DDYSTWDIVKATQYGIYERCRELVEAGYDVRQPDKENVTLLHWAAINNRIDLVKYYISKGAIVDQ--------------- 118
Cdd:PHA02876 175 DIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKndlsllkairnedle 254

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993 119 -------LGGDLNS------TPLHWATRQGHLS-MVVQLMKYGADPSLIDGEGCSCIHLAAQFGH-TSIVAYLIAKGQDV 183
Cdd:PHA02876 255 tslllydAGFSVNSiddcknTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADV 334

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993 184 DMMDQNGMTPLMWAAYRTHSVDPTRLLLTFNVSVNLGDKYHKnTALHWAVLAGNTTVISLLLEAGANVDAQNIKGESALD 263
Cdd:PHA02876 335 NAADRLYITPLHQASTLDRNKDIVITLLELGANVNARDYCDK-TPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALH 413

                        250
                 ....*....|
gi 103471993 264 LAKQRKNVWM 273
Cdd:PHA02876 414 FALCGTNPYM 423
PHA03095 PHA03095
ankyrin-like protein; Provisional
 76-275 5.62e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 71.59  E-value: 5.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993  76 LVEAGYDVRQPDKENVTLLHWAAINNRID--LVKYYISKGAIVdqlgGDLNS---TPLHWATRQGHLSM-VVQLM-KYGA 148
Cdd:PHA03095 103 LIKAGADVNAKDKVGRTPLHVYLSGFNINpkVIRLLLRKGADV----NALDLygmTPLAVLLKSRNANVeLLRLLiDAGA 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993 149 DPSLIDGEGCSCIHLAAQFGHTS--IVAYLIAKGQDVDMMDQNGMTPLMWAAyrTHSVDPTRLLLTF---NVSVNLGDKY 223
Cdd:PHA03095 179 DVYAVDDRFRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMA--TGSSCKRSLVLPLliaGISINARNRY 256

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 103471993 224 HKnTALHWAVLAGNTTVISLLLEAGANVDAQNIKGESALDLAKQRKNVWMIN 275
Cdd:PHA03095 257 GQ-TPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVR 307
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 104-268 5.63e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 71.45  E-value: 5.63e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993 104 DLVKYYISKGAIVDQLGGDLNSTPLHWATRQGHLSMVVQLMKYGADPSLIDGEGCSCIHLAAQFGHTSIVAYLIAKGQDV 183
Cdd:PHA02878 148 EITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAST 227

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993 184 DMMDQNGMTPLMWAAYRTHSVDPTRLLLTFNVSVNLGDKYHKNTALHWAVlaGNTTVISLLLEAGANVDAQNIKGESALD 263
Cdd:PHA02878 228 DARDKCGNTPLHISVGYCKDYDILKLLLEHGVDVNAKSYILGLTALHSSI--KSERKLKLLLEYGADINSLNSYKLTPLS 305


                 ....*.
gi 103471993 264 LA-KQR 268
Cdd:PHA02878 306 SAvKQY 311
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 53-265 3.14e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 66.24  E-value: 3.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993  53 IDDYSTWDIVKATQYGIYER-CRELVEAGYDVRQPDKENVTLLHWAAINN-RIDLVKYYISKGAIVDQlGGDLNSTPLHW 130
Cdd:PHA02876 269 IDDCKNTPLHHASQAPSLSRlVPKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNA-ADRLYITPLHQ 347

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993 131 A-TRQGHLSMVVQLMKYGADPSLIDGEGCSCIHLAAQFGHTSIVAYLIAKGQDVDMMDQNGMTPLMWAAYRTHSVDPTRL 209
Cdd:PHA02876 348 AsTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMSVKT 427

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 103471993 210 LLTFNVSVNLGDKYhKNTALHWAVLAG-NTTVISLLLEAGANVDAQNIKGESALDLA 265
Cdd:PHA02876 428 LIDRGANVNSKNKD-LSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIA 483
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 82-250 3.40e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 65.40  E-value: 3.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993  82 DVRQPDKEnvTLLHWAAINNRIDLVKYYISKGAIVDQLGGDLNSTPLHWATRQGHLSMVVQLMKYGADPSLIDGEGCSCI 161
Cdd:PHA02875  62 DVKYPDIE--SELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPL 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993 162 HLAAQFGHTSIVAYLIAKGQDVDMMDQNGMTPLMWA-AYRTHSVdpTRLLLTFNVSVNLGDKYHKNTALHWAVLAGNTTV 240
Cdd:PHA02875 140 HLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAmAKGDIAI--CKMLLDSGANIDYFGKNGCVAALCYAIENNKIDI 217

                        170
                 ....*....|
gi 103471993 241 ISLLLEAGAN 250
Cdd:PHA02875 218 VRLFIKRGAD 227
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 99-267 9.42e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 64.21  E-value: 9.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993  99 INNriDLVKYYISKGAIVDQLGGDLNsTPLHWATRQGHLSMVVQLMKYGADPSLIDGEGCSCIHLAAQFGHTSIVAYLIA 178
Cdd:PHA02874 102 IEK--DMIKTILDCGIDVNIKDAELK-TFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLE 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993 179 KGQDVDMMDQNGMTPLMWAA----YRThsvdpTRLLLTF--NVSVNLGDKYhknTALHWAVLAgNTTVISLLLEaGANVD 252
Cdd:PHA02874 179 KGAYANVKDNNGESPLHNAAeygdYAC-----IKLLIDHgnHIMNKCKNGF---TPLHNAIIH-NRSAIELLIN-NASIN 248

                        170
                 ....*....|....*
gi 103471993 253 AQNIKGESALDLAKQ 267
Cdd:PHA02874 249 DQDIDGSTPLHHAIN 263
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 133-264 1.19e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 64.70  E-value: 1.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993 133 RQGHLSMVVQLMKYGADPSLIDGEGCSCIHLAAQFGHTSIVAYLIAKGQDVDMMDQNGMTPLMWA--------------- 197
Cdd:PHA02876 154 QQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAvdsknidtikaiidn 233

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993 198 -------------AYRTHSVDPTRLLLTFNVSVNLGDKYhKNTALHWAVLAGN-TTVISLLLEAGANVDAQNIKGESALD 263
Cdd:PHA02876 234 rsninkndlsllkAIRNEDLETSLLLYDAGFSVNSIDDC-KNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLY 312


                 .
gi 103471993 264 L 264
Cdd:PHA02876 313 L 313
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 88-314 1.79e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 63.47  E-value: 1.79e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993  88 KENVTLLHWAAINNRIDLVKYYISKGAIVDQLGGDlNSTPLHWATRQGHLSMVVQLMKYGADPSLIDGEGCSCIHLAAQF 167
Cdd:PHA02875 100 KDGMTPLHLATILKKLDIMKLLIARGADPDIPNTD-KFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAK 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993 168 GHTSIVAYLIAKGQDVDMMDQNGMTPLMWAAYRTHSVDPTRLLLT----------------------FNVSVNLGD---- 221
Cdd:PHA02875 179 GDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIKrgadcnimfmiegeectildmiCNMCTNLESeaid 258

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993 222 --------KYHKNTALHWAVLAGNTTVI---SLLLEAGAN-------VDAQNIKGESALDLAKQRKNVWMINHLQEARQA 283
Cdd:PHA02875 259 aliadiaiRIHKKTIRRDEGFKNNMSTIedkEEFKDVFEKciielrrIKSEKIGKKNILDLCILEKNSHNLDENILARHS 338

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 103471993 284 KG----YDNPSFLRKL---KADKEFRQKVMLGTPFLVI 314
Cdd:PHA02875 339 KKilglNDEAHFYKYLlkeAADIALKRAEAIESAIRVI 376
PHA03095 PHA03095
ankyrin-like protein; Provisional
 74-295 4.23e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 62.35  E-value: 4.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993  74 RELVEAGYDVRQPDKENVTLLHWAAIN-NRIDLVKYYISKGAIVDQlGGDLNSTPLHwatrqghlsmvvqlmkygadpsl 152
Cdd:PHA03095  67 RLLLEAGADVNAPERCGFTPLHLYLYNaTTLDVIKLLIKAGADVNA-KDKVGRTPLH----------------------- 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993 153 idgegcscIHLAAQFGHTSIVAYLIAKGQDVDMMDQNGMTPLmwAAY-RTHSVDPT--RLLL-----TFNVSVNL----- 219
Cdd:PHA03095 123 --------VYLSGFNINPKVIRLLLRKGADVNALDLYGMTPL--AVLlKSRNANVEllRLLIdagadVYAVDDRFrsllh 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993 220 ------------------------GDKYHKNTALHWAVLAGN--TTVISLLLEAGANVDAQNIKGESALdlakqrknvwm 273
Cdd:PHA03095 193 hhlqsfkprarivreliragcdpaATDMLGNTPLHSMATGSSckRSLVLPLLIAGISINARNRYGQTPL----------- 261

                        250       260
                 ....*....|....*....|..
gi 103471993 274 inHLqearqAKGYDNPSFLRKL 295
Cdd:PHA03095 262 --HY-----AAVFNNPRACRRL 276
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 63-189 8.14e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 61.22  E-value: 8.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993  63 KATQYGIYErcrELVEAGYDVRQPDKENVTLLHWAAINNRIDL--VKYYISKGAIVDQ---------LGGDLNS------ 125
Cdd:PHA03100 117 KSNSYSIVE---YLLDNGANVNIKNSDGENLLHLYLESNKIDLkiLKLLIDKGVDINAknrvnyllsYGVPINIkdvygf 193

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 103471993 126 TPLHWATRQGHLSMVVQLMKYGADPSLIDGEGCSCIHLAAQFGHTSIVAYLIAKGQDVDMMDQN 189
Cdd:PHA03100 194 TPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 103-262 3.00e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 59.62  E-value: 3.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993 103 IDLVKYYISKGAIVDQLGGDLNStPLHWATRQGHLSMVVQLM---KYGADpsLIDGEGCSCIHLAAQFGHTSIVAYLIAK 179
Cdd:PHA02875  48 SEAIKLLMKHGAIPDVKYPDIES-ELHDAVEEGDVKAVEELLdlgKFADD--VFYKDGMTPLHLATILKKLDIMKLLIAR 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993 180 GQDVDMMDQNGMTPLMWAAYrTHSVDPTRLLLTFNVSVNLGDKYhKNTALHWAVLAGNTTVISLLLEAGANVDAQNIKGE 259
Cdd:PHA02875 125 GADPDIPNTDKFSPLHLAVM-MGDIKGIELLIDHKACLDIEDCC-GCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGC 202


                 ...
gi 103471993 260 SAL 262
Cdd:PHA02875 203 VAA 205
Ank_4 pfam13637
Ankyrin repeats (many copies);
124-177 3.97e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.66  E-value: 3.97e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 103471993  124 NSTPLHWATRQGHLSMVVQLMKYGADPSLIDGEGCSCIHLAAQFGHTSIVAYLI 177
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 135-307 1.55e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 57.96  E-value: 1.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993 135 GHLSMVVQLMKYGADPSLIDGEGCSCIHLAAQFGHTSIVAYLIAKGQDVDMMDQNGMTPlMWAAYRTHSVDPTRLLLTFn 214
Cdd:PLN03192 536 GNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTA-LWNAISAKHHKIFRILYHF- 613

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993 215 vsVNLGDKYHKNTALHWAVLAGNTTVISLLLEAGANVDAQNIKGESALDLAKQRKNVWMINHL----QEARQAKGYDN-- 288
Cdd:PLN03192 614 --ASISDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLimngADVDKANTDDDfs 691

                        170
                 ....*....|....*....
gi 103471993 289 PSFLRKLKADKEFRQKVML 307
Cdd:PLN03192 692 PTELRELLQKRELGHSITI 710
PHA03095 PHA03095
ankyrin-like protein; Provisional
 74-194 8.41e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 55.03  E-value: 8.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993  74 RELVEAGYDVRQPDKENVTLLHWAAINNRID--LVKYYISKGaiVDQLGGD-LNSTPLHWATRQGHL--SMVVQLMKYGA 148
Cdd:PHA03095 171 RLLIDAGADVYAVDDRFRSLLHHHLQSFKPRarIVRELIRAG--CDPAATDmLGNTPLHSMATGSSCkrSLVLPLLIAGI 248

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 103471993 149 DPSLIDGEGCSCIHLAAQFGHTSIVAYLIAKGQDVDMMDQNGMTPL 194
Cdd:PHA03095 249 SINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 126-271 9.84e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 54.61  E-value: 9.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993 126 TPLHWATRQGHLSMVVQLMKYGADPSLIDGEGCSCIHLAAQFGHTSIVAYLIAKGQDV-DMMDQNGMTPLmWAAYRTHSV 204
Cdd:PHA02875  37 SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAdDVFYKDGMTPL-HLATILKKL 115

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 103471993 205 DPTRLLLTFNVSVNLGDKyHKNTALHWAVLAGNTTVISLLLEAGANVDAQNIKGESALDLAKQRKNV 271
Cdd:PHA02875 116 DIMKLLIARGADPDIPNT-DKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDI 181
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 74-265 1.25e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 54.50  E-value: 1.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993  74 RELVEAGYDVRQPDKENVTLLHWAAINNRIDLVKYYISKgAIVDQLGGDLNSTPLHWATRQGHLSMVVQLMKYGADPSLI 153
Cdd:PHA02878  54 KSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRS-INKCSVFYTLVAIKDAFNNRNVEIFKIILTNRYKNIQTID 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993 154 DGEGCSCIHlaAQFGHTSIVAYLIAKGQDVDMMDQN-GMTPLMWAAyRTHSVDPTRLLLTFNVSVNLGDKYHkNTALHWA 232
Cdd:PHA02878 133 LVYIDKKSK--DDIIEAEITKLLLSYGADINMKDRHkGNTALHYAT-ENKDQRLTELLLSYGANVNIPDKTN-NSPLHHA 208

                        170       180       190
                 ....*....|....*....|....*....|...
gi 103471993 233 VLAGNTTVISLLLEAGANVDAQNIKGESALDLA 265
Cdd:PHA02878 209 VKHYNKPIVHILLENGASTDARDKCGNTPLHIS 241
Ank_5 pfam13857
Ankyrin repeats (many copies);
209-265 1.45e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.50  E-value: 1.45e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 103471993  209 LLLTFNVSVNLGDKyHKNTALHWAVLAGNTTVISLLLEAGANVDAQNIKGESALDLA 265
Cdd:pfam13857   1 LLEHGPIDLNRLDG-EGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
159-202 2.29e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.65  E-value: 2.29e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 103471993  159 SCIHLAAQFGHTSIVAYLIAKGQDVDMMDQNGMTPLMWAAYRTH 202
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGN 46
Ank_4 pfam13637
Ankyrin repeats (many copies);
90-140 2.56e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.65  E-value: 2.56e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 103471993   90 NVTLLHWAAINNRIDLVKYYISKGAIVDQLGGDLNsTPLHWATRQGHLSMV 140
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGE-TALHFAASNGNVEVL 50
PHA03095 PHA03095
ankyrin-like protein; Provisional
 74-187 2.19e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 50.41  E-value: 2.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993  74 RELVEAGYDVRQPDKENVTLLHWAAINN--RIDLVKYYISKGAIVDQLGgDLNSTPLHWATRQGHLSMVVQLMKYGADPS 151
Cdd:PHA03095 206 RELIRAGCDPAATDMLGNTPLHSMATGSscKRSLVLPLLIAGISINARN-RYGQTPLHYAAVFNNPRACRRLIALGADIN 284

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 103471993 152 LIDGEGCSCIHLAAQFGHTSIVAYLIAKGQDVDMMD 187
Cdd:PHA03095 285 AVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVA 320
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 120-190 7.33e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.13  E-value: 7.33e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 103471993 120 GGDLNS------TPLHWATRQGHLSMVVQLMKYGADPSLIDGEGCSCIHLAAQFGHTSIVAYLIAKGQDVDMMDQNG 190
Cdd:PTZ00322 105 GADPNCrdydgrTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGANA 181
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 224-255 7.61e-06

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 43.05  E-value: 7.61e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 103471993  224 HKNTALHWAVL-AGNTTVISLLLEAGANVDAQN 255
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
Ank_4 pfam13637
Ankyrin repeats (many copies);
226-265 2.60e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.88  E-value: 2.60e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 103471993  226 NTALHWAVLAGNTTVISLLLEAGANVDAQNIKGESALDLA 265
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFA 41
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 122-279 3.34e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 46.88  E-value: 3.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993 122 DLNSTPLHWATRQGHLSMVVQLMKYGADPSLIDGEGCSCIHLAAQFGHTSIVAYLIAKGQDVDMMDqngmTPLMwaayrt 201
Cdd:PHA02874  33 DETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSILP----IPCI------ 102

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 103471993 202 hSVDPTRLLLTFNVSVNLGDKYHKnTALHWAVLAGNTTVISLLLEAGANVDAQNIKGESALDLAKQRKNVWMINHLQE 279
Cdd:PHA02874 103 -EKDMIKTILDCGIDVNIKDAELK-TFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLE 178
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 143-194 8.85e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 45.66  E-value: 8.85e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 103471993 143 LMKYGADPSLIDGEGCSCIHLAAQFGHTSIVAYLIAKGQDVDMMDQNGMTPL 194
Cdd:PTZ00322 101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPL 152
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 126-256 1.36e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 45.24  E-value: 1.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993 126 TPLHWATRQGHLSMVVQLMKYGADPSLIDGEGCSCIHLAAQFGHTSI--VAYLIAKGQDvdmmDQNGMTPLMWAAYRtHS 203
Cdd:PLN03192 560 TPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIfrILYHFASISD----PHAAGDLLCTAAKR-ND 634

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 103471993 204 VDPTRLLLTFNVSVNLGDkYHKNTALHWAVLAGNTTVISLLLEAGANVDAQNI 256
Cdd:PLN03192 635 LTAMKELLKQGLNVDSED-HQGATALQVAMAEDHVDMVRLLIMNGADVDKANT 686
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 224-253 1.58e-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: 1.58e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 103471993   224 HKNTALHWAVLAGNTTVISLLLEAGANVDA 253
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_2 pfam12796
Ankyrin repeats (3 copies);
229-286 2.18e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 40.48  E-value: 2.18e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 103471993  229 LHWAVLAGNTTVISLLLEAGANVDAQNIKGESALDLAKQRKNV----WMINHLQEARQAKGY 286
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLeivkLLLEHADVNLKDNGR 62
Ank_5 pfam13857
Ankyrin repeats (many copies);
109-164 2.45e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.25  E-value: 2.45e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 103471993  109 YISKGAIVDQLGGDLNSTPLHWATRQGHLSMVVQLMKYGADPSLIDGEGCSCIHLA 164
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 208-267 2.59e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.12  E-value: 2.59e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993 208 RLLLTFNVSVNLGDkYHKNTALHWAVLAGNTTVISLLLEAGANVDAQNIKGESALDLAKQ 267
Cdd:PTZ00322  99 RILLTGGADPNCRD-YDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEE 157
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 94-270 2.72e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 43.72  E-value: 2.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993  94 LHWAAINNRIDLVKYYISKGAIVDQLGGDlNSTPLHWATRQGHLsmvvQLMKYGADPSLIDGEGCSCIHLAAQFGHTSIV 173
Cdd:PHA02878  41 LHQAVEARNLDVVKSLLTRGHNVNQPDHR-DLTPLHIICKEPNK----LGMKEMIRSINKCSVFYTLVAIKDAFNNRNVE 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993 174 aylIAKGQDVDMMDQNGMTPLMWaaYRTHSVDP------TRLLLTFNVSVNLGDKYHKNTALHWAVLAGNTTVISLLLEA 247
Cdd:PHA02878 116 ---IFKIILTNRYKNIQTIDLVY--IDKKSKDDiieaeiTKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSY 190

                        170       180
                 ....*....|....*....|...
gi 103471993 248 GANVDAQNIKGESALDLAKQRKN 270
Cdd:PHA02878 191 GANVNIPDKTNNSPLHHAVKHYN 213
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 70-194 3.73e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 43.70  E-value: 3.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993  70 YERC-RELVEAGYDVRQPDKENVTLLhWAAI---NNRIDLVKYYISkgAIVD-QLGGDLnstpLHWATRQGHLSMVVQLM 144
Cdd:PLN03192 570 YEDCvLVLLKHACNVHIRDANGNTAL-WNAIsakHHKIFRILYHFA--SISDpHAAGDL----LCTAAKRNDLTAMKELL 642

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 103471993 145 KYGADPSLIDGEGCSCIHLAAQFGHTSIVAYLIAKGQDVDMMD-QNGMTPL 194
Cdd:PLN03192 643 KQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANtDDDFSPT 693
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 126-154 5.79e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 37.65  E-value: 5.79e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 103471993  126 TPLHWA-TRQGHLSMVVQLMKYGADPSLID 154
Cdd:pfam00023   4 TPLHLAaGRRGNLEIVKLLLSKGADVNARD 33
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 135-281 6.75e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 42.67  E-value: 6.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993 135 GHLSMVVQLMKYGADPSLIDGEGCSCIHLAAQFGHTSIVAYLIAKGQDVDMMDQNGMTPLMWAAYRThSVDPTRLLLTFN 214
Cdd:PHA02875  13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEG-DVKAVEELLDLG 91

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 103471993 215 VSVNlgDKYHK--NTALHWAVLAGNTTVISLLLEAGANVDAQNIKGESALDLAKQRKNVWMINHLQEAR 281
Cdd:PHA02875  92 KFAD--DVFYKdgMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHK 158
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 224-253 7.03e-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: 7.03e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 103471993  224 HKNTALHWAVLAGNTTVISLLLEAGANVDA 253
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 156-187 8.75e-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: 8.75e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 103471993  156 EGCSCIHLAA-QFGHTSIVAYLIAKGQDVDMMD 187
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 122-269 8.88e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 40.96  E-value: 8.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993 122 DLNSTPLHWATRQGHLS--MVVQLMKYGADPS-LIDGEGCSCIHLAAQFGHT---SIVAYLIAKGQDVDMMDQNGMTPL- 194
Cdd:PHA02859  49 DLYETPIFSCLEKDKVNveILKFLIENGADVNfKTRDNNLSALHHYLSFNKNvepEILKILIDSGSSITEEDEDGKNLLh 128

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 103471993 195 MWAAYRTHSVDPTRLLLTFNVSVNLGDKYHKNTALHWAVLAGNTTVISLLLEAGANVDAQNIKGESALDLAKQRK 269
Cdd:PHA02859 129 MYMCNFNVRINVIKLLIDSGVSFLNKDFDNNNILYSYILFHSDKKIFDFLTSLGIDINETNKSGYNCYDLIKFRN 203
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 189-222 1.05e-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: 1.05e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 103471993  189 NGMTPLMWAAYRTHSVDPTRLLLTFNVSVNLGDK 222
Cdd:pfam00023   1 DGNTPLHLAAGRRGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 126-150 1.09e-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: 1.09e-03
                           10        20
                   ....*....|....*....|....*
gi 103471993   126 TPLHWATRQGHLSMVVQLMKYGADP 150
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADI 28
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 209-296 1.15e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 41.97  E-value: 1.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993 209 LLLTFNVSVNLGDKYHKnTALHWAVLAGNTTVISLLLEAGANVDAQNIKGESALDLAKQRKNVWMINHLQEARQAKGYDN 288
Cdd:PHA02876 163 MLLEGGADVNAKDIYCI-TPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKND 241


                 ....*...
gi 103471993 289 PSFLRKLK 296
Cdd:PHA02876 242 LSLLKAIR 249
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 92-117 1.26e-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: 1.26e-03
                          10        20
                  ....*....|....*....|....*.
gi 103471993   92 TLLHWAAINNRIDLVKYYISKGAIVD 117
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADIN 29
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 92-281 1.38e-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: 1.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993  92 TLLHWAAINNRIDLVKYYI--SKGAIVDQLGGDL--NSTPLHWATRQGHLSMVVQLMKYGADPS--------LIDGEGCS 159
Cdd:cd22192   53 TALHVAALYDNLEAAVVLMeaAPELVNEPMTSDLyqGETALHIAVVNQNLNLVRELIARGADVVspratgtfFRPGPKNL 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993 160 C------IHLAAQFGHTSIVAYLIAKGQDVDMMDQNGmtplmwaayrthsvdptrllltfnvsvnlgdkyhkNTALHWAV 233
Cdd:cd22192  133 IyygehpLSFAACVGNEEIVRLLIEHGADIRAQDSLG-----------------------------------NTVLHILV 177

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 103471993 234 LAGNTT----VISLLLEAGANVDAQ------NIKGESALDLAKQRKNVWMINHLQEAR 281
Cdd:cd22192  178 LQPNKTfacqMYDLILSYDKEDDLQpldlvpNNQGLTPFKLAAKEGNIVMFQHLVQKR 235
Ank_5 pfam13857
Ankyrin repeats (many copies);
148-194 1.38e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.33  E-value: 1.38e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 103471993  148 ADPSLIDGEGCSCIHLAAQFGHTSIVAYLIAKGQDVDMMDQNGMTPL 194
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 156-185 3.63e-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: 3.63e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 103471993   156 EGCSCIHLAAQFGHTSIVAYLIAKGQDVDM 185
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 64-188 5.81e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 39.56  E-value: 5.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103471993  64 ATQYGIYERCRELVEAGYDVRQPDKENVTLLHWAAINNRiDLVKYYISKGAIVDQlggDLN-STPLHWATRQGHLSMVVQ 142
Cdd:PHA02874 197 AAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLINNASINDQ---DIDgSTPLHHAINPPCDIDIID 272

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 103471993 143 LMKY-GADPSLIDGEGCSCIHLAAQF-GHTSIVAYLIAKGQDVDMMDQ 188
Cdd:PHA02874 273 ILLYhKADISIKDNKGENPIDTAFKYiNKDPVIKDIIANAVLIKEADK 320
Ank_5 pfam13857
Ankyrin repeats (many copies);
176-232 7.11e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.01  E-value: 7.11e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 103471993  176 LIAKGQ-DVDMMDQNGMTPLMWAAYRtHSVDPTRLLLTFNVSVNLGDKyHKNTALHWA 232
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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