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Conserved domains on  [gi|528479266|ref|XP_005171884|]
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ankyrin repeat family A protein 2 isoform X1 [Danio rerio]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 11429852)

ankyrin repeat domain-containing protein; ANK proteins mediate specific protein-protein interactions without necessarily recognizing specific primary sequences which allows for one ankyrin repeat domain to recognize and bind to a variety of intracellular substrates and may be involved in a wide array of functions

Gene Ontology:  GO:0005515
PubMed:  17176038
SCOP:  4000366

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
141-301 8.99e-41

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 143.17  E-value: 8.99e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479266 141 IHQLAAQGEMVFLASRIEQESVINLQDEEGFTPLMWAAAHGQIAVVEFLLQSGADPHLLAKGRESALSLACSKGYTDIVR 220
Cdd:COG0666   91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479266 221 MLIDCGVDVNEYDWNGGAPLLYAVHGNHVRCVEILLESGSDPTMESDSGFNAMDMAVAMGHRNVQQVLEAHLLKLLQGIK 300
Cdd:COG0666  171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250


                 .
gi 528479266 301 E 301
Cdd:COG0666  251 D 251
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
141-301 8.99e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 143.17  E-value: 8.99e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479266 141 IHQLAAQGEMVFLASRIEQESVINLQDEEGFTPLMWAAAHGQIAVVEFLLQSGADPHLLAKGRESALSLACSKGYTDIVR 220
Cdd:COG0666   91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479266 221 MLIDCGVDVNEYDWNGGAPLLYAVHGNHVRCVEILLESGSDPTMESDSGFNAMDMAVAMGHRNVQQVLEAHLLKLLQGIK 300
Cdd:COG0666  171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250


                 .
gi 528479266 301 E 301
Cdd:COG0666  251 D 251
Ank_2 pfam12796
Ankyrin repeats (3 copies);
174-263 3.38e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.94  E-value: 3.38e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479266  174 LMWAAAHGQIAVVEFLLQSGADPHLLAKGRESALSLACSKGYTDIVRMLIDCgVDVNEYDwNGGAPLLYAVHGNHVRCVE 253
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|
gi 528479266  254 ILLESGSDPT 263
Cdd:pfam12796  79 LLLEKGADIN 88
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 130-278 1.60e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 64.30  E-value: 1.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479266 130 SSTPLLVHSLSIHQLAAQGEMVFLAsrIEQESVINLQDEEGFTPLMWAAAH--GQIAVVEFLLQSGADPHLLAKGRESAL 207
Cdd:PHA03100  68 NSTPLHYLSNIKYNLTDVKEIVKLL--LEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLL 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479266 208 SLA--CSKGYTDIVRMLIDCGVDVN-----EY-----------DWNGGAPLLYAVHGNHVRCVEILLESGSDPTMESDSG 269
Cdd:PHA03100 146 HLYleSNKIDLKILKLLIDKGVDINaknrvNYllsygvpinikDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYG 225


                 ....*....
gi 528479266 270 FNAMDMAVA 278
Cdd:PHA03100 226 DTPLHIAIL 234
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 169-198 3.53e-06

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: 42.96  E-value: 3.53e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 528479266   169 EGFTPLMWAAAHGQIAVVEFLLQSGADPHL 198
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 169-240 1.31e-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: 40.38  E-value: 1.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479266 169 EGFTPLMWAAAHGQIAVVEFLLQSGAD--------------PHLLAKGRESALSLACSKGYTDIVRMLIDCGVDVNEYDW 234
Cdd:cd22192   88 QGETALHIAVVNQNLNLVRELIARGADvvspratgtffrpgPKNLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDS 167


                 ....*.
gi 528479266 235 NGGAPL 240
Cdd:cd22192  168 LGNTVL 173
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
141-301 8.99e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 143.17  E-value: 8.99e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479266 141 IHQLAAQGEMVFLASRIEQESVINLQDEEGFTPLMWAAAHGQIAVVEFLLQSGADPHLLAKGRESALSLACSKGYTDIVR 220
Cdd:COG0666   91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479266 221 MLIDCGVDVNEYDWNGGAPLLYAVHGNHVRCVEILLESGSDPTMESDSGFNAMDMAVAMGHRNVQQVLEAHLLKLLQGIK 300
Cdd:COG0666  171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250


                 .
gi 528479266 301 E 301
Cdd:COG0666  251 D 251
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
141-291 1.33e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 126.99  E-value: 1.33e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479266 141 IHQLAAQGEMVFLASRIEQESVINLQDEEGFTPLMWAAAHGQIAVVEFLLQSGADPHLLAKGRESALSLACSKGYTDIVR 220
Cdd:COG0666   58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528479266 221 MLIDCGVDVNEYDWNGGAPLLYAVHGNHVRCVEILLESGSDPTMESDSGFNAMDMAVAMGHRNVQQVLEAH 291
Cdd:COG0666  138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA 208
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
163-301 2.56e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 118.52  E-value: 2.56e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479266 163 INLQDEEGFTPLMWAAAHGQIAVVEFLLQSGADPHLLAKGRESALSLACSKGYTDIVRMLIDCGVDVNEYDWNGGAPLLY 242
Cdd:COG0666  146 VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDL 225

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 528479266 243 AVHGNHVRCVEILLESGSDPTMESDSGFNAMDMAVAMGHRNVQQVLEAHLLKLLQGIKE 301
Cdd:COG0666  226 AAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLD 284
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
134-291 2.20e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 94.25  E-value: 2.20e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479266 134 LLVHSLSIHQLAAQGEMVFLASRIEQESVINLQDEEGFTPLMWAAAHGQIAVVEFLLQSGADPHLLAKGRESALSLACSK 213
Cdd:COG0666   18 LLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARN 97

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528479266 214 GYTDIVRMLIDCGVDVNEYDWNGGAPLLYAVHGNHVRCVEILLESGSDPTMESDSGFNAMDMAVAMGHRNVQQVLEAH 291
Cdd:COG0666   98 GDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA 175
Ank_2 pfam12796
Ankyrin repeats (3 copies);
174-263 3.38e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.94  E-value: 3.38e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479266  174 LMWAAAHGQIAVVEFLLQSGADPHLLAKGRESALSLACSKGYTDIVRMLIDCgVDVNEYDwNGGAPLLYAVHGNHVRCVE 253
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|
gi 528479266  254 ILLESGSDPT 263
Cdd:pfam12796  79 LLLEKGADIN 88
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
163-273 9.95e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 86.93  E-value: 9.95e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479266 163 INLQDEEGFTPLMWAAAHGQIAVVEFLLQSGADPHLLAKGRESALSLACSKGYTDIVRMLIDCGVDVNEYDWNGGAPLLY 242
Cdd:COG0666  179 VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLL 258

                         90       100       110
                 ....*....|....*....|....*....|.
gi 528479266 243 AVHGNHVRCVEILLESGSDPTMESDSGFNAM 273
Cdd:COG0666  259 AAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
144-233 2.44e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.45  E-value: 2.44e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479266  144 LAAQGEMVFLASR-IEQESVINLQDEEGFTPLMWAAAHGQIAVVEFLLQSgADPHLLAKGReSALSLACSKGYTDIVRML 222
Cdd:pfam12796   3 LAAKNGNLELVKLlLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGR-TALHYAARSGHLEIVKLL 80

                          90
                  ....*....|.
gi 528479266  223 IDCGVDVNEYD 233
Cdd:pfam12796  81 LEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 130-278 1.60e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 64.30  E-value: 1.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479266 130 SSTPLLVHSLSIHQLAAQGEMVFLAsrIEQESVINLQDEEGFTPLMWAAAH--GQIAVVEFLLQSGADPHLLAKGRESAL 207
Cdd:PHA03100  68 NSTPLHYLSNIKYNLTDVKEIVKLL--LEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLL 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479266 208 SLA--CSKGYTDIVRMLIDCGVDVN-----EY-----------DWNGGAPLLYAVHGNHVRCVEILLESGSDPTMESDSG 269
Cdd:PHA03100 146 HLYleSNKIDLKILKLLIDKGVDINaknrvNYllsygvpinikDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYG 225


                 ....*....
gi 528479266 270 FNAMDMAVA 278
Cdd:PHA03100 226 DTPLHIAIL 234
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
152-291 2.69e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 59.97  E-value: 2.69e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479266 152 FLASRIEQESVINLQDEEGFTPLMWAAAHGQIAVVEFLLQSGADPHLLAKGRESALSLACSKGYTDIVRMLIDCGVDVNE 231
Cdd:COG0666    3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479266 232 YDWNGGAPLLYAVHGNHVRCVEILLESGSDPTMESDSGFNAMDMAVAMGHRNVQQVLEAH 291
Cdd:COG0666   83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA 142
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 133-236 1.09e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 59.14  E-value: 1.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479266 133 PLLVHSLSIH--QLAAQGEMVFLASRIEQESVINLQDEEGFTPLMWAAAHGQIAVVEFLLQSGADPHLLAKGRESALSLA 210
Cdd:PTZ00322  76 PVVAHMLTVElcQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA 155

                         90       100
                 ....*....|....*....|....*.
gi 528479266 211 CSKGYTDIVRMLIDCGVDVNEYDWNG 236
Cdd:PTZ00322 156 EENGFREVVQLLSRHSQCHFELGANA 181
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 157-266 3.16e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 57.31  E-value: 3.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479266 157 IEQESVINLQDEEGFTPLMWAAAHGQIAVVEFLLQSGADPHLLAK-GRESALSLACSKGYTDIVRMLIDCGVDVNeydwn 235
Cdd:PHA02875 155 IDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKnGCVAALCYAIENNKIDIVRLFIKRGADCN----- 229

                         90       100       110
                 ....*....|....*....|....*....|.
gi 528479266 236 ggapLLYAVHGNHVRCVEILLESGSDPTMES 266
Cdd:PHA02875 230 ----IMFMIEGEECTILDMICNMCTNLESEA 256
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 163-288 3.59e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 57.28  E-value: 3.59e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479266 163 INLQDEEGFTPLMWAAAHGQIAVVEFLLQSGADPHLLAKGRESALSLACSKGYTDIVRMLI------------------- 223
Cdd:PHA02874  28 INISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIdngvdtsilpipciekdmi 107

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528479266 224 ----DCGVDVNEYDWNGGAPLLYAVHGNHVRCVEILLESGSDPTMESDSGFNAMDMAVAMGHRNVQQVL 288
Cdd:PHA02874 108 ktilDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLL 176
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 157-296 6.12e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 56.60  E-value: 6.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479266 157 IEQESVINLQDEEGFTPLMWAAAHGQIAVVEFLLQSGADPHLLAKGRESALSLACSKGYT-----DIVRMLIDCGVDVNE 231
Cdd:PHA03100  22 IMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNA 101

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528479266 232 YDWNGGAPLLYAV--HGNHVRCVEILLESGSDPTMESDSGFNAMDMAVAMGHRNVQqvleahLLKLL 296
Cdd:PHA03100 102 PDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLK------ILKLL 162
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 157-230 8.10e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 56.21  E-value: 8.10e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528479266 157 IEQESVINLQDEEGFTPLMWAAAHGQIAVVEFLLQSGADPHLLAKGRESALSLACSKGYTDIVRMLIDCGVDVN 230
Cdd:PHA03100 179 LSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 163-277 3.62e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 54.20  E-value: 3.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479266 163 INLQDEEGFTPLMWAAAHGQIAVVEFLLQSGADPHLLAKGRESALSLACSKGYTDIVRMLIDCGVDVNEYDWNGGAPLLY 242
Cdd:PHA02874 117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 528479266 243 AVHGNHVRCVEILLESGSDPTMESDSGFNAMDMAV 277
Cdd:PHA02874 197 AAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI 231
Ank_4 pfam13637
Ankyrin repeats (many copies);
203-256 5.28e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.42  E-value: 5.28e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 528479266  203 RESALSLACSKGYTDIVRMLIDCGVDVNEYDWNGGAPLLYAVHGNHVRCVEILL 256
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 219-291 8.79e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.36  E-value: 8.79e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528479266 219 VRMLIDCGVDVNEYDWNGGAPLLYAVHGNHVRCVEILLESGSDPTMESDSGFNAMDMAVAMGHRNVQQVLEAH 291
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 168-269 1.12e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 52.69  E-value: 1.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479266 168 EEGFTPLMWAAAHGQIAVVEFLLQSGADPHLLAKGRESALSLACSKGYTDIVRMLIDCGVDVNEYDWNGGAPLLYAVHGN 247
Cdd:PHA02875 100 KDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKG 179

                         90       100
                 ....*....|....*....|..
gi 528479266 248 HVRCVEILLESGSDPTMESDSG 269
Cdd:PHA02875 180 DIAICKMLLDSGANIDYFGKNG 201
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 164-291 2.02e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 51.92  E-value: 2.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479266 164 NLQDEEGFTPLMWAAAHGQIAVVEFLLQSGADPHLLAKGRESALSLACSKGYTDIVRMLIDCGVDVNEYDW-NGGAPLLY 242
Cdd:PHA02875  29 NFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYkDGMTPLHL 108

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 528479266 243 AVHGNHVRCVEILLESGSDPTMESDSGFNAMDMAVAMGHRNVQQVLEAH 291
Cdd:PHA02875 109 ATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDH 157
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 114-267 2.30e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 52.18  E-value: 2.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479266 114 IKQST---TLTNKHRGNEVSSTPLLVHSLSIHQLAAQGemvFLASRIEQESVINLQDEegftpLMWAAAHGQIAVVEFLL 190
Cdd:PLN03192 474 LKTSTlieAMQTRQEDNVVILKNFLQHHKELHDLNVGD---LLGDNGGEHDDPNMASN-----LLTVASTGNAALLEELL 545

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479266 191 QSGADPHLL-AKGReSALSLACSKGYTDIVRMLIDCGVDVNEYDWNGGAPLLYAVHGNHVRCVEIL--LESGSDPTMESD 267
Cdd:PLN03192 546 KAKLDPDIGdSKGR-TPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILyhFASISDPHAAGD 624
Ank_4 pfam13637
Ankyrin repeats (many copies);
172-223 2.88e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.50  E-value: 2.88e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 528479266  172 TPLMWAAAHGQIAVVEFLLQSGADPHLLAKGRESALSLACSKGYTDIVRMLI 223
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 163-277 4.84e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 50.65  E-value: 4.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479266 163 INLQDEE-GFTPLMWAAAHGQIAVVEFLLQSGADPHLLAKGRESALSLACSKGYTDIVRMLIDCGVDVNEYDWNGGAPLL 241
Cdd:PHA02878 160 INMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLH 239

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 528479266 242 YAV-HGNHVRCVEILLESGSDPTMESD-SGFNAMDMAV 277
Cdd:PHA02878 240 ISVgYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSI 277
PHA03095 PHA03095
ankyrin-like protein; Provisional
 127-223 6.10e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 50.41  E-value: 6.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479266 127 NEVSSTPLlvHSLSIHQLAAQGEMVFLasrIEQESVINLQDEEGFTPLMWAAAHGQIAVVEFLLQSGADPHLLAKGRESA 206
Cdd:PHA03095 219 DMLGNTPL--HSMATGSSCKRSLVLPL---LIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTP 293

                         90
                 ....*....|....*..
gi 528479266 207 LSLACSKGYTDIVRMLI 223
Cdd:PHA03095 294 LSLMVRNNNGRAVRAAL 310
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
132-240 1.70e-06

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 48.41  E-value: 1.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479266 132 TPLlvhslsiHQLAAQG--EMV-FLasrIEQESVINLQDEEGFTPLMWAAAHGQIAVVEFLLQSGADPHLLAKGRESALS 208
Cdd:COG0666  188 TPL-------HLAAENGhlEIVkLL---LEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALL 257

                         90       100       110
                 ....*....|....*....|....*....|..
gi 528479266 209 LACSKGYTDIVRMLIDCGVDVNEYDWNGGAPL 240
Cdd:COG0666  258 LAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
121-198 1.93e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 45.49  E-value: 1.93e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528479266  121 TNKHRGNEVSSTPLlvhslsihQLAAQGEMVFLASRIEQESVINLQDEeGFTPLMWAAAHGQIAVVEFLLQSGADPHL 198
Cdd:pfam12796  21 ADANLQDKNGRTAL--------HLAAKNGHLEIVKLLLEHADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINV 89
Ank_5 pfam13857
Ankyrin repeats (many copies);
163-210 2.25e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.26  E-value: 2.25e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 528479266  163 INLQDEEGFTPLMWAAAHGQIAVVEFLLQSGADPHLLAKGRESALSLA 210
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 169-198 3.53e-06

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: 42.96  E-value: 3.53e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 528479266   169 EGFTPLMWAAAHGQIAVVEFLLQSGADPHL 198
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
239-288 5.05e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.03  E-value: 5.05e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 528479266  239 PLLYAVHGNHVRCVEILLESGSDPTMESDSGFNAMDMAVAMGHRNVQQVL 288
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 157-289 6.18e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 47.27  E-value: 6.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479266 157 IEQESVINLQDEEGFTPLMWAAAHGQIAVVEFLLQSGadphllakgreSALSLACSKGYT----------DIVRMLIDcG 226
Cdd:PHA02874 177 LEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHG-----------NHIMNKCKNGFTplhnaiihnrSAIELLIN-N 244

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528479266 227 VDVNEYDWNGGAPLLYAVHGN-HVRCVEILLESGSDPTMESDSGFNAMDmaVAMGHRNVQQVLE 289
Cdd:PHA02874 245 ASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPID--TAFKYINKDPVIK 306
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 178-256 9.02e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.82  E-value: 9.02e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528479266 178 AAHGQIAVVEFLLQSGADPHLLAKGRESALSLACSKGYTDIVRMLIDCGVDVNEYDWNGGAPLLYAVHGNHVRCVEILL 256
Cdd:PTZ00322  90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
PHA03095 PHA03095
ankyrin-like protein; Provisional
 163-296 1.23e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.56  E-value: 1.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479266 163 INLQDEEGFTPL---MWAAAHGQIAVVEFLLQSGADphLLAKGRESALSL---ACSKGYTDIVRMLIDCGVDVNEYDWNG 236
Cdd:PHA03095  40 VNFRGEYGKTPLhlyLHYSSEKVKDIVRLLLEAGAD--VNAPERCGFTPLhlyLYNATTLDVIKLLIKAGADVNAKDKVG 117

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528479266 237 GAPL-LYAVHGN-HVRCVEILLESGSDPTMESDSGFNAMDmaVAMGHRNVqqvlEAHLLKLL 296
Cdd:PHA03095 118 RTPLhVYLSGFNiNPKVIRLLLRKGADVNALDLYGMTPLA--VLLKSRNA----NVELLRLL 173
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 169-198 1.32e-05

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: 41.51  E-value: 1.32e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 528479266  169 EGFTPLMWAAAH-GQIAVVEFLLQSGADPHL 198
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNA 31
Ank_5 pfam13857
Ankyrin repeats (many copies);
189-243 1.35e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 1.35e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 528479266  189 LLQSG-ADPHLLAKGRESALSLACSKGYTDIVRMLIDCGVDVNEYDWNGGAPLLYA 243
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 114-259 1.48e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.21  E-value: 1.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479266 114 IKQSTTLTNKHR--------------GNEVSSTPL---LVHSLSIHQLAAQGEMVFLASRIEQESVINLQDEEGFTPLMW 176
Cdd:PHA02876 105 IKYASIILNKHKldeacihilkeaisGNDIHYDKInesIEYMKLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHY 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479266 177 AAAHGQIAVVEFLLQSGADPHLLAKGRESALSLACSKGYTDIVRMLIDCGVDVNEYDWNggapLLYAVHGNHVRCVEILL 256
Cdd:PHA02876 185 AAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNDLS----LLKAIRNEDLETSLLLY 260


                 ...
gi 528479266 257 ESG 259
Cdd:PHA02876 261 DAG 263
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 169-197 2.67e-05

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: 40.32  E-value: 2.67e-05
                          10        20
                  ....*....|....*....|....*....
gi 528479266  169 EGFTPLMWAAAHGQIAVVEFLLQSGADPH 197
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
Ank_5 pfam13857
Ankyrin repeats (many copies);
222-276 4.18e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.41  E-value: 4.18e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 528479266  222 LIDCG-VDVNEYDWNGGAPLLYAVHGNHVRCVEILLESGSDPTMESDSGFNAMDMA 276
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
137-190 6.39e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.95  E-value: 6.39e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 528479266  137 HSLSIHQLAAQGEMVFLASRIEQESVINLQDEEGFTPLMWAAAHGQIAVVEFLL 190
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 184-282 1.16e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 43.47  E-value: 1.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479266 184 AVVEFLLQSGADPHLLAKGRESAL-SLA--CSKGYTDIVRMLIDcGVDVNEYDWNGGAPLLYA-VHGNHVRCVEiLLESG 259
Cdd:PHA03095 203 RIVRELIRAGCDPAATDMLGNTPLhSMAtgSSCKRSLVLPLLIA-GISINARNRYGQTPLHYAaVFNNPRACRR-LIALG 280

                         90       100
                 ....*....|....*....|...
gi 528479266 260 SDPTMESDSGFNAMDMAVAMGHR 282
Cdd:PHA03095 281 ADINAVSSDGNTPLSLMVRNNNG 303
PHA02798 PHA02798
ankyrin-like protein; Provisional
 185-296 2.89e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 42.13  E-value: 2.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479266 185 VVEFLLQSGADPHLLAKGRESALSLACS-----KGYTDIVRMLIDCGVDVNEYDWNGGAPLLYAVHGNHVRCVEILL--- 256
Cdd:PHA02798  53 IVKLFINLGANVNGLDNEYSTPLCTILSnikdyKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLfmi 132

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 528479266 257 ESGSDPTMESDSGFNAMDMAVAMGHRnvqqvLEAHLLKLL 296
Cdd:PHA02798 133 ENGADTTLLDKDGFTMLQVYLQSNHH-----IDIEIIKLL 167
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 182-275 3.24e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 42.04  E-value: 3.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479266 182 QIAVVEFLLQSGADPH--------LLAKGRESALSlacSKGYTDIVRMLIDCGVDVNEYDWNGGAPLLYAVHGNHVRCVE 253
Cdd:PHA02989  49 KIKIVKLLIDNGADVNykgyietpLCAVLRNREIT---SNKIKKIVKLLLKFGADINLKTFNGVSPIVCFIYNSNINNCD 125

                         90       100
                 ....*....|....*....|....*.
gi 528479266 254 IL---LESGSD-PTMESDSGFNAMDM 275
Cdd:PHA02989 126 MLrflLSKGINvNDVKNSRGYNLLHM 151
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 204-231 8.73e-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: 36.08  E-value: 8.73e-04
                          10        20
                  ....*....|....*....|....*...
gi 528479266  204 ESALSLACSKGYTDIVRMLIDCGVDVNE 231
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 185-262 9.40e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 39.80  E-value: 9.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479266 185 VVEFLLQSGADPHLLAKGRE-SALS--LACSKGYT-DIVRMLIDCGVDVNEYDWNGGAPL-LYAVHGN-HVRCVEILLES 258
Cdd:PHA02859  68 ILKFLIENGADVNFKTRDNNlSALHhyLSFNKNVEpEILKILIDSGSSITEEDEDGKNLLhMYMCNFNvRINVIKLLIDS 147


                 ....
gi 528479266 259 GSDP 262
Cdd:PHA02859 148 GVSF 151
Ank_2 pfam12796
Ankyrin repeats (3 copies);
240-284 9.64e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 37.79  E-value: 9.64e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 528479266  240 LLYAVHGNHVRCVEILLESGSDPTMESDSGFNAMDMAVAMGHRNV 284
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEI 45
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 185-296 9.70e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 40.63  E-value: 9.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479266 185 VVEFLLQSGADPHLLAKGR-ESALSLACSKGYTDIVRMLIDCGVDVNEYDWNGGAPLLYAVHGNHVRCVEILLESGSDPT 263
Cdd:PHA02878 149 ITKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTD 228

                         90       100       110
                 ....*....|....*....|....*....|...
gi 528479266 264 MESDSGFNAMdmavamgHRNVQQVLEAHLLKLL 296
Cdd:PHA02878 229 ARDKCGNTPL-------HISVGYCKDYDILKLL 254
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 172-288 1.27e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 39.97  E-value: 1.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479266 172 TPLMWAAAHGQIAVVEFLLQSG--ADPHLLAKGReSALSLACSKGYTDIVRMLIDCGVDVNEYDWNGGAPLLYAVHGNHV 249
Cdd:PHA02875  70 SELHDAVEEGDVKAVEELLDLGkfADDVFYKDGM-TPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI 148

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 528479266 250 RCVEILLESGSDPTMESDSGFNAMDMAVAMGHRNVQQVL 288
Cdd:PHA02875 149 KGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKML 187
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 169-240 1.31e-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: 40.38  E-value: 1.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479266 169 EGFTPLMWAAAHGQIAVVEFLLQSGAD--------------PHLLAKGRESALSLACSKGYTDIVRMLIDCGVDVNEYDW 234
Cdd:cd22192   88 QGETALHIAVVNQNLNLVRELIARGADvvspratgtffrpgPKNLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDS 167


                 ....*.
gi 528479266 235 NGGAPL 240
Cdd:cd22192  168 LGNTVL 173
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 157-261 1.38e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 40.05  E-value: 1.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479266 157 IEQESVINLQDEEGFTPLMWAAAHG-QIAVVEFLLQSGADPHLLAKGRESALSLACS-KGYTDIVRMLIDCGVDVNEYDW 234
Cdd:PHA02876 294 LERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDY 373

                         90       100
                 ....*....|....*....|....*..
gi 528479266 235 NGGAPLLYAVHGNHVRCVEILLESGSD 261
Cdd:PHA02876 374 CDKTPIHYAAVRNNVVIINTLLDYGAD 400
PHA03095 PHA03095
ankyrin-like protein; Provisional
 183-295 1.74e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 39.62  E-value: 1.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479266 183 IAVVEFLLQSGADPHLLAKGRESAL-SLACS-KGYTDIVRMLIDCGVDVNEYDWNGGAPLLYAVHGNHVRCVEI--LLES 258
Cdd:PHA03095 167 VELLRLLIDAGADVYAVDDRFRSLLhHHLQSfKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIA 246

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 528479266 259 GSDPTMESDSGFNAMDMAVamGHRNvqQVLEAHLLKL 295
Cdd:PHA03095 247 GISINARNRYGQTPLHYAA--VFNN--PRACRRLIAL 279
PHA02791 PHA02791
ankyrin-like protein; Provisional
 167-257 1.88e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 39.25  E-value: 1.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479266 167 DEEGFTPLMWAAAHGQIAVVEFLLQSGADPHLLAKgrESALSLACSKGYTDIVRMLIDCGVDVNEYDWNGGAPLLYAVHG 246
Cdd:PHA02791  27 DVHGHSALYYAIADNNVRLVCTLLNAGALKNLLEN--EFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDS 104

                         90
                 ....*....|.
gi 528479266 247 NHVRCVEILLE 257
Cdd:PHA02791 105 GNMQTVKLFVK 115
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 163-261 2.18e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 39.47  E-value: 2.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479266 163 INLQDEEGFTPlMW---AAAHGQIAVVEFLLQSGADPHllAKGreSALSLACSKGYTDIVRMLIDCGVDVNEYDWNGGAP 239
Cdd:PLN03192 584 VHIRDANGNTA-LWnaiSAKHHKIFRILYHFASISDPH--AAG--DLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATA 658

                         90       100
                 ....*....|....*....|..
gi 528479266 240 LLYAVHGNHVRCVEILLESGSD 261
Cdd:PLN03192 659 LQVAMAEDHVDMVRLLIMNGAD 680
PHA02792 PHA02792
ankyrin-like protein; Provisional
 185-299 5.07e-03

ankyrin-like protein; Provisional


Pssm-ID: 165155 [Multi-domain]  Cd Length: 631  Bit Score: 38.39  E-value: 5.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479266 185 VVEFLLQSGAD---------------PHLLAKGRESALSLACSKGYTDivrmlidcgvDVNEYDWNGGAPLLYAVHGNHV 249
Cdd:PHA02792 354 VVEYILKNGNVvvedddniinimplfPTLSIHESDVLSILKLCKPYID----------DINKIDKHGRSILYYCIESHSV 423

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 528479266 250 RCVEILLESGSDPTMESDSGFNAMDMAVAMGHRNVQQVLEAHlLKLLQGI 299
Cdd:PHA02792 424 SLVEWLIDNGADINITTKYGSTCIGICVILAHACIPEIAELY-IKILEII 472
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 205-231 5.64e-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: 33.72  E-value: 5.64e-03
                           10        20
                   ....*....|....*....|....*..
gi 528479266   205 SALSLACSKGYTDIVRMLIDCGVDVNE 231
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 204-233 6.81e-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: 33.80  E-value: 6.81e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 528479266  204 ESALSLACSK-GYTDIVRMLIDCGVDVNEYD 233
Cdd:pfam00023   3 NTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
 
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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