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Conserved domains on  [gi|388453839|ref|NP_001253310|]
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ankyrin repeat family A protein 2 [Macaca mulatta]

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];
169-313 5.10e-41

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 144.33  E-value: 5.10e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453839 169 IEQENVINHTDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQLLGKGRESALSLACSKGYTDIVKMLLDCGVDVNEYDWNG 248
Cdd:COG0666  107 LEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDG 186

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 388453839 249 GTPLLYAVHGNHVKCVKMLLESGADPTIETDSGYNSMDLAVALGYRSVQQVIESHLLKLLQNIKE 313
Cdd:COG0666  187 ETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKD 251
PLN03192 super family cl33658
Voltage-dependent potassium channel; Provisional
 93-207 2.67e-03

Voltage-dependent potassium channel; Provisional


The actual alignment was detected with superfamily member PLN03192:

Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 39.47  E-value: 2.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453839  93 VLFKAECNIHTSPSPGIQVrhVYTPSTTKH---FSPIKQSTTLTNKHRGNEVSTTPLLANSLSVHQlaaqgEMLYLATRI 169
Cdd:PLN03192 576 VLLKHACNVHIRDANGNTA--LWNAISAKHhkiFRILYHFASISDPHAAGDLLCTAAKRNDLTAMK-----ELLKQGLNV 648

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 388453839 170 EQEnvinhtDEEGFTPLMWAAAHGQIAVVEFLLQNGAD 207
Cdd:PLN03192 649 DSE------DHQGATALQVAMAEDHVDMVRLLIMNGAD 680
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
169-313 5.10e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 144.33  E-value: 5.10e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453839 169 IEQENVINHTDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQLLGKGRESALSLACSKGYTDIVKMLLDCGVDVNEYDWNG 248
Cdd:COG0666  107 LEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDG 186

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 388453839 249 GTPLLYAVHGNHVKCVKMLLESGADPTIETDSGYNSMDLAVALGYRSVQQVIESHLLKLLQNIKE 313
Cdd:COG0666  187 ETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKD 251
Ank_2 pfam12796
Ankyrin repeats (3 copies);
186-276 1.99e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.10  E-value: 1.99e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453839  186 LMWAAAHGQIAVVEFLLQNGADPQLLGKGRESALSLACSKGYTDIVKMLLDCgVDVNEYDwNGGTPLLYAVHGNHVKCVK 265
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|.
gi 388453839  266 MLLESGADPTI 276
Cdd:pfam12796  79 LLLEKGADINV 89
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 175-290 1.08e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 73.93  E-value: 1.08e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453839 175 INHTDEEGFTPLMWAAAH--GQIAVVEFLLQNGADPQLLGKGRESALSLA--CSKGYTDIVKMLLDCGVDVN-----EY- 244
Cdd:PHA03100  99 VNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYleSNKIDLKILKLLIDKGVDINaknrvNYl 178

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 388453839 245 ----------DWNGGTPLLYAVHGNHVKCVKMLLESGADPTIETDSGYNSMDLAVA 290
Cdd:PHA03100 179 lsygvpinikDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAIL 234
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 181-208 9.43e-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: 41.80  E-value: 9.43e-06
                           10        20
                   ....*....|....*....|....*...
gi 388453839   181 EGFTPLMWAAAHGQIAVVEFLLQNGADP 208
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 181-252 4.80e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 41.54  E-value: 4.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453839 181 EGFTPLMWAAAHGQIAVVEFLLQNGADPQ---------LLGKGR-----ESALSLACSKGYTDIVKMLLDCGVDVNEYDW 246
Cdd:cd22192   88 QGETALHIAVVNQNLNLVRELIARGADVVspratgtffRPGPKNliyygEHPLSFAACVGNEEIVRLLIEHGADIRAQDS 167


                 ....*.
gi 388453839 247 NGGTPL 252
Cdd:cd22192  168 LGNTVL 173
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 157-273 1.18e-03

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 40.45  E-value: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453839  157 AAQGEMLYLATRIEQENV---INHTDEEGFTPLMWAAAHGQ-IAVVEFLLQNGADPQLlGKgresALSLACSKGYTDIVK 232
Cdd:TIGR00870  24 AAERGDLASVYRDLEEPKklnINCPDRLGRSALFVAAIENEnLELTELLLNLSCRGAV-GD----TLLHAISLEYVDAVE 98

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 388453839  233 MLL----------DCGVDVNEYDWN----GGTPLLYAVHGNHVKCVKMLLESGAD 273
Cdd:TIGR00870  99 AILlhllaafrksGPLELANDQYTSeftpGITALHLAAHRQNYEIVKLLLERGAS 153
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 93-207 2.67e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 39.47  E-value: 2.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453839  93 VLFKAECNIHTSPSPGIQVrhVYTPSTTKH---FSPIKQSTTLTNKHRGNEVSTTPLLANSLSVHQlaaqgEMLYLATRI 169
Cdd:PLN03192 576 VLLKHACNVHIRDANGNTA--LWNAISAKHhkiFRILYHFASISDPHAAGDLLCTAAKRNDLTAMK-----ELLKQGLNV 648

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 388453839 170 EQEnvinhtDEEGFTPLMWAAAHGQIAVVEFLLQNGAD 207
Cdd:PLN03192 649 DSE------DHQGATALQVAMAEDHVDMVRLLIMNGAD 680
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
169-313 5.10e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 144.33  E-value: 5.10e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453839 169 IEQENVINHTDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQLLGKGRESALSLACSKGYTDIVKMLLDCGVDVNEYDWNG 248
Cdd:COG0666  107 LEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDG 186

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 388453839 249 GTPLLYAVHGNHVKCVKMLLESGADPTIETDSGYNSMDLAVALGYRSVQQVIESHLLKLLQNIKE 313
Cdd:COG0666  187 ETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKD 251
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
154-293 2.05e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 126.99  E-value: 2.05e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453839 154 HQLAAQGEMLYLATRIEQENVINHTDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQLLGKGRESALSLACSKGYTDIVKM 233
Cdd:COG0666   59 LAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKL 138

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453839 234 LLDCGVDVNEYDWNGGTPLLYAVHGNHVKCVKMLLESGADPTIETDSGYNSMDLAVALGY 293
Cdd:COG0666  139 LLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGH 198
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
146-313 3.99e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 120.83  E-value: 3.99e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453839 146 LLANSLSVHQLAAQGE-MLYLATRIEQENV----------INHTDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQLLGKG 214
Cdd:COG0666  106 LLEAGADVNARDKDGEtPLHLAAYNGNLEIvkllleagadVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDND 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453839 215 RESALSLACSKGYTDIVKMLLDCGVDVNEYDWNGGTPLLYAVHGNHVKCVKMLLESGADPTIETDSGYNSMDLAVALGYR 294
Cdd:COG0666  186 GETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAA 265

                        170
                 ....*....|....*....
gi 388453839 295 SVQQVIESHLLKLLQNIKE 313
Cdd:COG0666  266 LIVKLLLLALLLLAAALLD 284
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
146-293 1.42e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 97.72  E-value: 1.42e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453839 146 LLANSLSVHQLAAQGEMLYLATRIEQENVINHTDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQLLGKGRESALSLACSK 225
Cdd:COG0666   18 LLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARN 97

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 388453839 226 GYTDIVKMLLDCGVDVNEYDWNGGTPLLYAVHGNHVKCVKMLLESGADPTIETDSGYNSMDLAVALGY 293
Cdd:COG0666   98 GDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165
Ank_2 pfam12796
Ankyrin repeats (3 copies);
186-276 1.99e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.10  E-value: 1.99e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453839  186 LMWAAAHGQIAVVEFLLQNGADPQLLGKGRESALSLACSKGYTDIVKMLLDCgVDVNEYDwNGGTPLLYAVHGNHVKCVK 265
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|.
gi 388453839  266 MLLESGADPTI 276
Cdd:pfam12796  79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
156-245 2.39e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.14  E-value: 2.39e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453839  156 LAAQGEMLYLATR-IEQENVINHTDEEGFTPLMWAAAHGQIAVVEFLLQNgADPQLLGKGReSALSLACSKGYTDIVKML 234
Cdd:pfam12796   3 LAAKNGNLELVKLlLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGR-TALHYAARSGHLEIVKLL 80

                          90
                  ....*....|.
gi 388453839  235 LDCGVDVNEYD 245
Cdd:pfam12796  81 LEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 175-290 1.08e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 73.93  E-value: 1.08e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453839 175 INHTDEEGFTPLMWAAAH--GQIAVVEFLLQNGADPQLLGKGRESALSLA--CSKGYTDIVKMLLDCGVDVN-----EY- 244
Cdd:PHA03100  99 VNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYleSNKIDLKILKLLIDKGVDINaknrvNYl 178

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 388453839 245 ----------DWNGGTPLLYAVHGNHVKCVKMLLESGADPTIETDSGYNSMDLAVA 290
Cdd:PHA03100 179 lsygvpinikDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAIL 234
Ank_2 pfam12796
Ankyrin repeats (3 copies);
219-296 1.37e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.52  E-value: 1.37e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 388453839  219 LSLACSKGYTDIVKMLLDCGVDVNEYDWNGGTPLLYAVHGNHVKCVKMLLESgADPTIeTDSGYNSMDLAVALGYRSV 296
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNL-KDNGRTALHYAARSGHLEI 76
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 173-289 7.27e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 65.76  E-value: 7.27e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453839 173 NVINHTDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQLLGKGRESALSLACSKGYTDIVKML------------------ 234
Cdd:PHA02874  26 NCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLidngvdtsilpipciekd 105

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453839 235 -----LDCGVDVNEYDWNGGTPLLYAVHGNHVKCVKMLLESGADPTIETDSGYNSMDLAV 289
Cdd:PHA02874 106 miktiLDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAI 165
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
162-296 2.96e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 63.05  E-value: 2.96e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453839 162 MLYLATRIEQENVINHTDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQLLGKGRESALSLACSKGYTDIVKMLLDCGVDV 241
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 388453839 242 NEYDWNGGTPLLYAVHGNHVKCVKMLLESGADPTIETDSGYNSMDLAVALGYRSV 296
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI 135
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 184-308 1.49e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 61.60  E-value: 1.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453839 184 TPLMWAAAHGQIAVVEFLLQNGADPQLLGKGRESALSLACSKGYT-----DIVKMLLDCGVDVNEYDWNGGTPLLYAV-- 256
Cdd:PHA03100  37 LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAIsk 116

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 388453839 257 HGNHVKCVKMLLESGADPTIETDSGYNSMDLAVALGYrsvqqvIESHLLKLL 308
Cdd:PHA03100 117 KSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNK------IDLKILKLL 162
Ank_4 pfam13637
Ankyrin repeats (many copies);
215-268 2.75e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.97  E-value: 2.75e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 388453839  215 RESALSLACSKGYTDIVKMLLDCGVDVNEYDWNGGTPLLYAVHGNHVKCVKMLL 268
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 180-274 4.46e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 60.00  E-value: 4.46e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453839 180 EEGFTPLMWAAAHGQIAVVEFLLQNGADPQLLGKGRESALSLACSKGYTDIVKMLLDCGVDVNEYDWNGGTPLLYAVHGN 259
Cdd:PHA02875 100 KDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKG 179

                         90
                 ....*....|....*
gi 388453839 260 HVKCVKMLLESGADP 274
Cdd:PHA02875 180 DIAICKMLLDSGANI 194
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 231-303 2.14e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 58.37  E-value: 2.14e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 388453839 231 VKMLLDCGVDVNEYDWNGGTPLLYAVHGNHVKCVKMLLESGADPTIETDSGYNSMDLAVALGYRSVQQVIESH 303
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 140-248 4.52e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.22  E-value: 4.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453839 140 EVSTTPLLANSLSVH--QLAAQGEMLYLATRIEQENVINHTDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQLLGKGRES 217
Cdd:PTZ00322  71 EEVIDPVVAHMLTVElcQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKT 150

                         90       100       110
                 ....*....|....*....|....*....|.
gi 388453839 218 ALSLACSKGYTDIVKMLLDCGVDVNEYDWNG 248
Cdd:PTZ00322 151 PLELAEENGFREVVQLLSRHSQCHFELGANA 181
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 163-278 8.28e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 56.15  E-value: 8.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453839 163 LYLATRIEQENV------------INHTDEegFTPLMWAAAHGQIAVVEFLLQNGADPQLLGKGRESALSLACSKGYTDI 230
Cdd:PHA02875 106 LHLATILKKLDImklliargadpdIPNTDK--FSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAI 183

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 388453839 231 VKMLLDCGVDVNEYDWNGGTPLL-YAVHGNHVKCVKMLLESGADPTIET 278
Cdd:PHA02875 184 CKMLLDSGANIDYFGKNGCVAALcYAIENNKIDIVRLFIKRGADCNIMF 232
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 175-296 2.30e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 54.97  E-value: 2.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453839 175 INHTDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQLLGKGRESALSLACSKGYTDIVKMLLDCGVDVNEYDWNGGTPLLY 254
Cdd:PHA02874 117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 388453839 255 AVHGNHVKCVKMLLESGADPTIETDSGYNSMDLAVaLGYRSV 296
Cdd:PHA02874 197 AAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI-IHNRSA 237
PHA03095 PHA03095
ankyrin-like protein; Provisional
 175-308 2.42e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 55.03  E-value: 2.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453839 175 INHTDEEGFTPL---MWAAAHGQIAVVEFLLQNGADPQLLGKGRESAL-SLACSKGYTDIVKMLLDCGVDVNEYDWNGGT 250
Cdd:PHA03095  40 VNFRGEYGKTPLhlyLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLhLYLYNATTLDVIKLLIKAGADVNAKDKVGRT 119

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453839 251 PL-LYAVHGN-HVKCVKMLLESGADPTIETDSGYNSMDLAValgyRSVQQVIEshLLKLL 308
Cdd:PHA03095 120 PLhVYLSGFNiNPKVIRLLLRKGADVNALDLYGMTPLAVLL----KSRNANVE--LLRLL 173
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 176-292 2.45e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 54.61  E-value: 2.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453839 176 NHTDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQLLGKGRESALSLACSKGYTDIVKMLLDCGVDVNEYDW-NGGTPLLY 254
Cdd:PHA02875  29 NFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYkDGMTPLHL 108

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 388453839 255 AVHGNHVKCVKMLLESGADPTIETDSGYNSMDLAVALG 292
Cdd:PHA02875 109 ATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMG 146
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 175-242 2.56e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 54.67  E-value: 2.56e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 388453839 175 INHTDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQLLGKGRESALSLACSKGYTDIVKMLLDCGVDVN 242
Cdd:PHA03100 185 INIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 175-278 3.21e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 54.50  E-value: 3.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453839 175 INHTDEE-GFTPLMWAAAHGQIAVVEFLLQNGADPQLLGKGRESALSLACSKGYTDIVKMLLDCGVDVNEYDWNGGTPLL 253
Cdd:PHA02878 160 INMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLH 239

                         90       100
                 ....*....|....*....|....*.
gi 388453839 254 YAV-HGNHVKCVKMLLESGADPTIET 278
Cdd:PHA02878 240 ISVgYCKDYDILKLLLEHGVDVNAKS 265
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 175-301 5.61e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.81  E-value: 5.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453839 175 INHTDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQLLG---------------------KGRESA--LSLACSKGYTDIV 231
Cdd:PHA02874  61 INHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSILPipciekdmiktildcgidvniKDAELKtfLHYAIKKGDLESI 140

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 388453839 232 KMLLDCGVDVNEYDWNGGTPLLYAVHGNHVKCVKMLLESGADPTIETDSGYNSMDLAVALG-YRSVQQVIE 301
Cdd:PHA02874 141 KMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGdYACIKLLID 211
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 126-279 7.02e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 53.72  E-value: 7.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453839 126 IKQST---TLTNKHRGNEVSTTPLLANSLSVHQLAAqGEMLYlatrieqENVINHTDEEGFTPLMWAAAHGQIAVVEFLL 202
Cdd:PLN03192 474 LKTSTlieAMQTRQEDNVVILKNFLQHHKELHDLNV-GDLLG-------DNGGEHDDPNMASNLLTVASTGNAALLEELL 545

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453839 203 QNGADPQLL-GKGReSALSLACSKGYTDIVKMLLDCGVDVNEYDWNGGTPLLYAVHGNHVKCVKML--LESGADPTIETD 279
Cdd:PLN03192 546 KAKLDPDIGdSKGR-TPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILyhFASISDPHAAGD 624
Ank_4 pfam13637
Ankyrin repeats (many copies);
184-235 1.17e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.65  E-value: 1.17e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 388453839  184 TPLMWAAAHGQIAVVEFLLQNGADPQLLGKGRESALSLACSKGYTDIVKMLL 235
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
201-255 1.59e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.34  E-value: 1.59e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 388453839  201 LLQNG-ADPQLLGKGRESALSLACSKGYTDIVKMLLDCGVDVNEYDWNGGTPLLYA 255
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
175-222 5.81e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.80  E-value: 5.81e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 388453839  175 INHTDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQLLGKGRESALSLA 222
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_2 pfam12796
Ankyrin repeats (3 copies);
146-208 1.38e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 45.88  E-value: 1.38e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 388453839  146 LLANSLSVHQLAAQGEM-LYLATRIEQENV----INHTD----EEGFTPLMWAAAHGQIAVVEFLLQNGADP 208
Cdd:pfam12796  16 LLENGADANLQDKNGRTaLHLAAKNGHLEIvkllLEHADvnlkDNGRTALHYAARSGHLEIVKLLLEKGADI 87
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 198-278 2.08e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 48.89  E-value: 2.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453839 198 VEFLLQNGADPQLLGKGRESALSLACSKGYTDIVKMLLDCGVDVNEYDWNGGTPLLYAVHGNHVKCVKMLLESGadPTIE 277
Cdd:PHA03100 175 VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNG--PSIK 252


                 .
gi 388453839 278 T 278
Cdd:PHA03100 253 T 253
Ank_5 pfam13857
Ankyrin repeats (many copies);
234-288 3.48e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.49  E-value: 3.48e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 388453839  234 LLDCG-VDVNEYDWNGGTPLLYAVHGNHVKCVKMLLESGADPTIETDSGYNSMDLA 288
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
169-252 4.99e-06

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 47.26  E-value: 4.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453839 169 IEQENVINHTDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQLLGKGRESALSLACSKGYTDIVKMLLDCGVDVNEYDWNG 248
Cdd:COG0666  206 LEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285


                 ....
gi 388453839 249 GTPL 252
Cdd:COG0666  286 LTLL 289
Ank_4 pfam13637
Ankyrin repeats (many copies);
153-202 8.88e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.26  E-value: 8.88e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 388453839  153 VHQLAAQGEMLYLATRIEQENVINHTDEEGFTPLMWAAAHGQIAVVEFLL 202
Cdd:pfam13637   5 LHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 181-208 9.43e-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: 41.80  E-value: 9.43e-06
                           10        20
                   ....*....|....*....|....*...
gi 388453839   181 EGFTPLMWAAAHGQIAVVEFLLQNGADP 208
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 169-288 1.47e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 46.11  E-value: 1.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453839 169 IEQENVINHTDEEGFTPLMWAAAHGQIAVVEFLLQNGadpqllgkgreSALSLACSKGYT----------DIVKMLLDcG 238
Cdd:PHA02874 177 LEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHG-----------NHIMNKCKNGFTplhnaiihnrSAIELLIN-N 244

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 388453839 239 VDVNEYDWNGGTPLLYAVHGN-HVKCVKMLLESGADPTIETDSGYNSMDLA 288
Cdd:PHA02874 245 ASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTA 295
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 181-208 1.70e-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: 41.09  E-value: 1.70e-05
                          10        20
                  ....*....|....*....|....*...
gi 388453839  181 EGFTPLMWAAAHGQIAVVEFLLQNGADP 208
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 181-208 2.02e-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: 40.74  E-value: 2.02e-05
                          10        20
                  ....*....|....*....|....*....
gi 388453839  181 EGFTPLMWAAAH-GQIAVVEFLLQNGADP 208
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADV 29
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 194-283 2.28e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 45.89  E-value: 2.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453839 194 QIAVVEFLLQNGADPQLLG----------KGRESAlslacSKGYTDIVKMLLDCGVDVNEYDWNGGTPL---LYAVHGNH 260
Cdd:PHA02989  49 KIKIVKLLIDNGADVNYKGyietplcavlRNREIT-----SNKIKKIVKLLLKFGADINLKTFNGVSPIvcfIYNSNINN 123

                         90       100
                 ....*....|....*....|....
gi 388453839 261 VKCVKMLLESGAD-PTIETDSGYN 283
Cdd:PHA02989 124 CDMLRFLLSKGINvNDVKNSRGYN 147
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 126-293 2.37e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.82  E-value: 2.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453839 126 IKQSTTLTNKHRGNEVSTTPLL----ANSLSVHQLAAQGE-MLYLATRIEQENV------------INHTDEEGFTPLMW 188
Cdd:PHA02876 105 IKYASIILNKHKLDEACIHILKeaisGNDIHYDKINESIEyMKLIKERIQQDELliaemlleggadVNAKDIYCITPIHY 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453839 189 AAAHGQIAVVEFLLQNGADPQLLGKGRESALSLACSKGYTDIVK-----------------------------MLLDCGV 239
Cdd:PHA02876 185 AAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKaiidnrsninkndlsllkairnedletslLLYDAGF 264

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 388453839 240 DVNEYDWNGGTPLLYAVHGNHV-KCVKMLLESGADPTIETDSGYNSMDLAVALGY 293
Cdd:PHA02876 265 SVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAKNGY 319
PHA03095 PHA03095
ankyrin-like protein; Provisional
 175-235 5.18e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 44.63  E-value: 5.18e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 388453839 175 INHTDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQLLGKGRESALSLACSKGYTDIVKMLL 235
Cdd:PHA03095 250 INARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 197-301 6.52e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 43.27  E-value: 6.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453839 197 VVEFLLQNGADPQLLGKGRE-SALS--LACSKGYT-DIVKMLLDCGVDVNEYDWNGGTPL-LYAVHGN-HVKCVKMLLES 270
Cdd:PHA02859  68 ILKFLIENGADVNFKTRDNNlSALHhyLSFNKNVEpEILKILIDSGSSITEEDEDGKNLLhMYMCNFNvRINVIKLLIDS 147

                         90       100       110
                 ....*....|....*....|....*....|.
gi 388453839 271 GADPtIETDSGYNSMdLAVALGYRSVQQVIE 301
Cdd:PHA02859 148 GVSF-LNKDFDNNNI-LYSYILFHSDKKIFD 176
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 247-279 7.02e-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: 39.19  E-value: 7.02e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 388453839  247 NGGTPLLYAV-HGNHVKCVKMLLESGADPTIETD 279
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA02798 PHA02798
ankyrin-like protein; Provisional
 197-308 9.19e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 43.67  E-value: 9.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453839 197 VVEFLLQNGADpqLLGKGRESALSLaCS--------KGYTDIVKMLLDCGVDVNEYDWNGGTPLLYAVHG---NHVKCVK 265
Cdd:PHA02798  53 IVKLFINLGAN--VNGLDNEYSTPL-CTilsnikdyKHMLDIVKILIENGADINKKNSDGETPLYCLLSNgyiNNLEILL 129

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 388453839 266 MLLESGADPTIETDSGYNSMDLAVALGYRsvqqvIESHLLKLL 308
Cdd:PHA02798 130 FMIENGADTTLLDKDGFTMLQVYLQSNHH-----IDIEIIKLL 167
PHA02792 PHA02792
ankyrin-like protein; Provisional
 197-311 9.89e-05

ankyrin-like protein; Provisional


Pssm-ID: 165155 [Multi-domain]  Cd Length: 631  Bit Score: 43.78  E-value: 9.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453839 197 VVEFLLQNGAD---------------PQLLGKGRESALSLACSKGYTDivkmlldcgvDVNEYDWNGGTPLLYAVHGNHV 261
Cdd:PHA02792 354 VVEYILKNGNVvvedddniinimplfPTLSIHESDVLSILKLCKPYID----------DINKIDKHGRSILYYCIESHSV 423

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 388453839 262 KCVKMLLESGADPTIETDSGYNSMDLAVALGYRSVQQVIESHlLKLLQNI 311
Cdd:PHA02792 424 SLVEWLIDNGADINITTKYGSTCIGICVILAHACIPEIAELY-IKILEII 472
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 175-301 1.99e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 42.74  E-value: 1.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453839 175 INHTDEEGFTPLMWAAAHG-QIAVVEFLLQNGADPQLLGKGRESALSLACS-KGYTDIVKMLLDCGVDVNEYDWNGGTPL 252
Cdd:PHA02876 300 VNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPI 379

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 388453839 253 LYAVHGNHVKCVKMLLESGADptIETDSGYNSMDLAVAL----GYRSVQQVIE 301
Cdd:PHA02876 380 HYAAVRNNVVIINTLLDYGAD--IEALSQKIGTALHFALcgtnPYMSVKTLID 430
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 175-300 2.13e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 42.93  E-value: 2.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453839 175 INHTDEEGFTPlMW---AAAHGQIAVVEFLLQNGADPQLLGkgreSALSLACSKGYTDIVKMLLDCGVDVNEYDWNGGTP 251
Cdd:PLN03192 584 VHIRDANGNTA-LWnaiSAKHHKIFRILYHFASISDPHAAG----DLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATA 658

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 388453839 252 LLYAVHGNHVKCVKMLLESGADPT-IETDSGYNSMDLAVALGYRSVQQVI 300
Cdd:PLN03192 659 LQVAMAEDHVDMVRLLIMNGADVDkANTDDDFSPTELRELLQKRELGHSI 708
PHA02791 PHA02791
ankyrin-like protein; Provisional
 179-269 2.33e-04

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 41.95  E-value: 2.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453839 179 DEEGFTPLMWAAAHGQIAVVEFLLQNGADPQLLGKgrESALSLACSKGYTDIVKMLLDCGVDVNEYDWNGGTPLLYAVHG 258
Cdd:PHA02791  27 DVHGHSALYYAIADNNVRLVCTLLNAGALKNLLEN--EFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDS 104

                         90
                 ....*....|.
gi 388453839 259 NHVKCVKMLLE 269
Cdd:PHA02791 105 GNMQTVKLFVK 115
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 247-276 2.58e-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: 37.57  E-value: 2.58e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 388453839   247 NGGTPLLYAVHGNHVKCVKMLLESGADPTI 276
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 184-300 2.71e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 42.29  E-value: 2.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453839 184 TPLMWAAAHGQIAVVEFLLQNG--ADPQLLGKGReSALSLACSKGYTDIVKMLLDCGVDVNEYDWNGGTPLLYAVHGNHV 261
Cdd:PHA02875  70 SELHDAVEEGDVKAVEELLDLGkfADDVFYKDGM-TPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI 148

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 388453839 262 KCVKMLLESGADPTIETDSGYNSMDLAVALGYRSVQQVI 300
Cdd:PHA02875 149 KGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKML 187
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 181-252 4.80e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 41.54  E-value: 4.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453839 181 EGFTPLMWAAAHGQIAVVEFLLQNGADPQ---------LLGKGR-----ESALSLACSKGYTDIVKMLLDCGVDVNEYDW 246
Cdd:cd22192   88 QGETALHIAVVNQNLNLVRELIARGADVVspratgtffRPGPKNliyygEHPLSFAACVGNEEIVRLLIEHGADIRAQDS 167


                 ....*.
gi 388453839 247 NGGTPL 252
Cdd:cd22192  168 LGNTVL 173
Ank_4 pfam13637
Ankyrin repeats (many copies);
248-296 7.00e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.87  E-value: 7.00e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 388453839  248 GGTPLLYAVHGNHVKCVKMLLESGADPTIETDSGYNSMDLAVALGYRSV 296
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEV 49
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 184-273 7.87e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 41.15  E-value: 7.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453839 184 TPLMWAAAHGQI-AVVEFLLQNGADPQLLGKGRESALSLACSKGYTDIVKMLLDCGVD-VNE------YDwnGGTPLLYA 255
Cdd:cd22192   19 SPLLLAAKENDVqAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEpmtsdlYQ--GETALHIA 96

                         90
                 ....*....|....*...
gi 388453839 256 VHGNHVKCVKMLLESGAD 273
Cdd:cd22192   97 VVNQNLNLVRELIARGAD 114
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 216-243 1.00e-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: 36.08  E-value: 1.00e-03
                          10        20
                  ....*....|....*....|....*...
gi 388453839  216 ESALSLACSKGYTDIVKMLLDCGVDVNE 243
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02798 PHA02798
ankyrin-like protein; Provisional
 195-286 1.15e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 40.20  E-value: 1.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453839 195 IAVVEFLLQNGADPQLLGKGRESALSLACSKGYT---DIVKMLLDCGVDVNEYDWNGGTPL-LYAVHGNHV--KCVKMLL 268
Cdd:PHA02798  89 LDIVKILIENGADINKKNSDGETPLYCLLSNGYInnlEILLFMIENGADTTLLDKDGFTMLqVYLQSNHHIdiEIIKLLL 168

                         90
                 ....*....|....*....
gi 388453839 269 ESGAD-PTIETDSGYNSMD 286
Cdd:PHA02798 169 EKGVDiNTHNNKEKYDTLH 187
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 157-273 1.18e-03

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 40.45  E-value: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453839  157 AAQGEMLYLATRIEQENV---INHTDEEGFTPLMWAAAHGQ-IAVVEFLLQNGADPQLlGKgresALSLACSKGYTDIVK 232
Cdd:TIGR00870  24 AAERGDLASVYRDLEEPKklnINCPDRLGRSALFVAAIENEnLELTELLLNLSCRGAV-GD----TLLHAISLEYVDAVE 98

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 388453839  233 MLL----------DCGVDVNEYDWN----GGTPLLYAVHGNHVKCVKMLLESGAD 273
Cdd:TIGR00870  99 AILlhllaafrksGPLELANDQYTSeftpGITALHLAAHRQNYEIVKLLLERGAS 153
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 197-308 1.45e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 40.25  E-value: 1.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453839 197 VVEFLLQNGADPQLLGKGR-ESALSLACSKGYTDIVKMLLDCGVDVNEYDWNGGTPLLYAVHGNHVKCVKMLLESGAdpT 275
Cdd:PHA02878 149 ITKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA--S 226

                         90       100       110
                 ....*....|....*....|....*....|...
gi 388453839 276 IETDSGYNSMDLAVALGYrsvqqVIESHLLKLL 308
Cdd:PHA02878 227 TDARDKCGNTPLHISVGY-----CKDYDILKLL 254
PHA03095 PHA03095
ankyrin-like protein; Provisional
 175-290 1.49e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 40.01  E-value: 1.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453839 175 INHTDEEGFTPL------MWAAAhgqiAVVEFLLQNGADPQ--------------------------LLGKG-------- 214
Cdd:PHA03095 110 VNAKDKVGRTPLhvylsgFNINP----KVIRLLLRKGADVNaldlygmtplavllksrnanvellrlLIDAGadvyavdd 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453839 215 -RESAL-SLACS-KGYTDIVKMLLD------------------------C-----------GVDVNEYDWNGGTPLLYA- 255
Cdd:PHA03095 186 rFRSLLhHHLQSfKPRARIVRELIRagcdpaatdmlgntplhsmatgssCkrslvlplliaGISINARNRYGQTPLHYAa 265

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 388453839 256 VHGNHVKCVKmLLESGADPTIETDSGYNSMDLAVA 290
Cdd:PHA03095 266 VFNNPRACRR-LIALGADINAVSSDGNTPLSLMVR 299
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 247-276 2.65e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.93  E-value: 2.65e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 388453839  247 NGGTPLLYAVHGNHVKCVKMLLESGADPTI 276
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 93-207 2.67e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 39.47  E-value: 2.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453839  93 VLFKAECNIHTSPSPGIQVrhVYTPSTTKH---FSPIKQSTTLTNKHRGNEVSTTPLLANSLSVHQlaaqgEMLYLATRI 169
Cdd:PLN03192 576 VLLKHACNVHIRDANGNTA--LWNAISAKHhkiFRILYHFASISDPHAAGDLLCTAAKRNDLTAMK-----ELLKQGLNV 648

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 388453839 170 EQEnvinhtDEEGFTPLMWAAAHGQIAVVEFLLQNGAD 207
Cdd:PLN03192 649 DSE------DHQGATALQVAMAEDHVDMVRLLIMNGAD 680
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 66-273 3.16e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 39.28  E-value: 3.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453839  66 SRFVKSLNEE----DSKNIQDQVNSDLeVASVLFKAEcNIHTSPSPGIQVrhvyTPSTTKHFSPIKQSTTLtNKHRGNEV 141
Cdd:PHA02876 287 SRLVPKLLERgadvNAKNIKGETPLYL-MAKNGYDTE-NIRTLIMLGADV----NAADRLYITPLHQASTL-DRNKDIVI 359

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453839 142 STTPLLAN--------SLSVHQLAAQGEMLYLATRIEQENVINHTDEEGFTPLMWA-AAHGQIAVVEFLLQNGADPQLLG 212
Cdd:PHA02876 360 TLLELGANvnardycdKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKN 439

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 388453839 213 KGRESALSLACSKG-YTDIVKMLLDCGVDVNEYDWNGGTPLLYAVHGNHVkcVKMLLESGAD 273
Cdd:PHA02876 440 KDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIALEYHGI--VNILLHYGAE 499
PHA02798 PHA02798
ankyrin-like protein; Provisional
 169-242 3.77e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 38.66  E-value: 3.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453839 169 IEQENVINHTDEEGFTPLMWAAAHGQIAVVEFLL---QNGADPQLLGKGRESALSLACSKGYT---DIVKMLLDCGVDVN 242
Cdd:PHA02798  96 IENGADINKKNSDGETPLYCLLSNGYINNLEILLfmiENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDIN 175
PHA02795 PHA02795
ankyrin-like protein; Provisional
 229-308 4.11e-03

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 38.44  E-value: 4.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453839 229 DIVKMLLDCGVDVNEYDWNGGTPLLYAVHGNHVKCVKMLLESGADPTIETDSGYNSMDLAVALGYRSVQQVIESHLLKLL 308
Cdd:PHA02795 202 EIYKLCIPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRGSVIARRETHLKILEIL 281
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 53-282 4.14e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 38.71  E-value: 4.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453839  53 KFILPNRFDMNVCSRFVkslnEEDSKNIQDQVnsDLEVASVLFK--AECNIHTspspgiqvRHvyTPSTTKHFSPIKQST 130
Cdd:PHA02878 118 KIILTNRYKNIQTIDLV----YIDKKSKDDII--EAEITKLLLSygADINMKD--------RH--KGNTALHYATENKDQ 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453839 131 TLTNK--HRGNEVSTtPLLANSLSVHQLAAQGEMLYLATRIEQENVINHTDEEGFTPLMWAAAH-GQIAVVEFLLQNGAD 207
Cdd:PHA02878 182 RLTELllSYGANVNI-PDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVD 260

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453839 208 PQLLGKGRE-SALSLACSKgyTDIVKMLLDCGVDVNEYDWNGGTPLLYAVHGNH-VKCVKML-----LESGADPTIETDS 280
Cdd:PHA02878 261 VNAKSYILGlTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSAVKQYLcINIGRILisnicLLKRIKPDIKNSE 338


                 ..
gi 388453839 281 GY 282
Cdd:PHA02878 339 GF 340
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 217-243 4.86e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.10  E-value: 4.86e-03
                           10        20
                   ....*....|....*....|....*..
gi 388453839   217 SALSLACSKGYTDIVKMLLDCGVDVNE 243
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 216-245 5.48e-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: 34.19  E-value: 5.48e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 388453839  216 ESALSLACSK-GYTDIVKMLLDCGVDVNEYD 245
Cdd:pfam00023   3 NTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
PHA02798 PHA02798
ankyrin-like protein; Provisional
 179-281 6.75e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 37.89  E-value: 6.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453839 179 DEEGFTPL---MWAAAHGQIAVVEFLLQNGADPQLLGKgRESALSLACSKGYT------DIVKMLLDCG----------- 238
Cdd:PHA02798 142 DKDGFTMLqvyLQSNHHIDIEIIKLLLEKGVDINTHNN-KEKYDTLHCYFKYNidridaDILKLFVDNGfiinkenkshk 220

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 388453839 239 ----------------------------VDVNEYDWNGGTPLLYAVHGNHVKCVKMLLESGADPTIETDSG 281
Cdd:PHA02798 221 kkfmeylnsllydnkrfkknildfifsyIDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELG 291
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 197-300 7.56e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 37.66  E-value: 7.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453839 197 VVEFLLQNGADPQLLGKGRESA----LSLACSKGYTDIVKMLLDCGVDVNEY-DWNGGTPLLYAVHGNHVKCVKMLLESG 271
Cdd:PHA02884  48 IIDAILKLGADPEAPFPLSENSktnpLIYAIDCDNDDAAKLLIRYGADVNRYaEEAKITPLYISVLHGCLKCLEILLSYG 127

                         90       100
                 ....*....|....*....|....*....
gi 388453839 272 ADPTIETDSGYNSMDLAVALGYRSVQQVI 300
Cdd:PHA02884 128 ADINIQTNDMVTPIELALMICNNFLAFMI 156
 
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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