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Conserved domains on  [gi|966947269|ref|XP_014995685|]
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ankyrin repeat family A protein 2 isoform X1 [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];
101-245 1.73e-41

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 143.17  E-value: 1.73e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966947269 101 IEQENVINHTDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQLLGKGRESALSLACSKGYTDIVKMLLDCGVDVNEYDWNG 180
Cdd:COG0666  107 LEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDG 186

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966947269 181 GTPLLYAVHGNHVKCVKMLLESGADPTIETDSGYNSMDLAVALGYRSVQQVIESHLLKLLQNIKE 245
Cdd:COG0666  187 ETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKD 251
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
101-245 1.73e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 143.17  E-value: 1.73e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966947269 101 IEQENVINHTDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQLLGKGRESALSLACSKGYTDIVKMLLDCGVDVNEYDWNG 180
Cdd:COG0666  107 LEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDG 186

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966947269 181 GTPLLYAVHGNHVKCVKMLLESGADPTIETDSGYNSMDLAVALGYRSVQQVIESHLLKLLQNIKE 245
Cdd:COG0666  187 ETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKD 251
Ank_2 pfam12796
Ankyrin repeats (3 copies);
118-208 1.36e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.95  E-value: 1.36e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966947269  118 LMWAAAHGQIAVVEFLLQNGADPQLLGKGRESALSLACSKGYTDIVKMLLDCgVDVNEYDwNGGTPLLYAVHGNHVKCVK 197
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|.
gi 966947269  198 MLLESGADPTI 208
Cdd:pfam12796  79 LLLEKGADINV 89
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 107-222 1.07e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 72.78  E-value: 1.07e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966947269 107 INHTDEEGFTPLMWAAAH--GQIAVVEFLLQNGADPQLLGKGRESALSLACSKGYTDI------------------VKML 166
Cdd:PHA03100  99 VNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkilkllidkgvdinaknrVNYL 178

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 966947269 167 LDCGVDVNEYDWNGGTPLLYAVHGNHVKCVKMLLESGADPTIETDSGYNSMDLAVA 222
Cdd:PHA03100 179 LSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAIL 234
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 113-140 1.16e-05

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: 41.03  E-value: 1.16e-05
                           10        20
                   ....*....|....*....|....*...
gi 966947269   113 EGFTPLMWAAAHGQIAVVEFLLQNGADP 140
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 113-184 4.36e-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: 4.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966947269 113 EGFTPLMWAAAHGQIAVVEFLLQNGADPQ---------LLGKGR-----ESALSLACSKGYTDIVKMLLDCGVDVNEYDW 178
Cdd:cd22192   88 QGETALHIAVVNQNLNLVRELIARGADVVspratgtffRPGPKNliyygEHPLSFAACVGNEEIVRLLIEHGADIRAQDS 167


                 ....*.
gi 966947269 179 NGGTPL 184
Cdd:cd22192  168 LGNTVL 173
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 89-205 9.86e-04

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: 40.06  E-value: 9.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966947269   89 AAQGEMLYLATRIEQENV---INHTDEEGFTPLMWAAAHGQ-IAVVEFLLQNGADPQLlGKgresALSLACSKGYTDIVK 164
Cdd:TIGR00870  24 AAERGDLASVYRDLEEPKklnINCPDRLGRSALFVAAIENEnLELTELLLNLSCRGAV-GD----TLLHAISLEYVDAVE 98

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 966947269  165 MLL----------DCGVDVNEYDWN----GGTPLLYAVHGNHVKCVKMLLESGAD 205
Cdd:TIGR00870  99 AILlhllaafrksGPLELANDQYTSeftpGITALHLAAHRQNYEIVKLLLERGAS 153
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
101-245 1.73e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 143.17  E-value: 1.73e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966947269 101 IEQENVINHTDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQLLGKGRESALSLACSKGYTDIVKMLLDCGVDVNEYDWNG 180
Cdd:COG0666  107 LEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDG 186

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966947269 181 GTPLLYAVHGNHVKCVKMLLESGADPTIETDSGYNSMDLAVALGYRSVQQVIESHLLKLLQNIKE 245
Cdd:COG0666  187 ETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKD 251
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
86-225 7.31e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 126.22  E-value: 7.31e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966947269  86 HQLAAQGEMLYLATRIEQENVINHTDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQLLGKGRESALSLACSKGYTDIVKM 165
Cdd:COG0666   59 LAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKL 138

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 966947269 166 LLDCGVDVNEYDWNGGTPLLYAVHGNHVKCVKMLLESGADPTIETDSGYNSMDLAVALGY 225
Cdd:COG0666  139 LLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGH 198
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
78-245 1.50e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 120.06  E-value: 1.50e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966947269  78 LLANSLSVHQLAAQGE-MLYLATRIEQENV----------INHTDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQLLGKG 146
Cdd:COG0666  106 LLEAGADVNARDKDGEtPLHLAAYNGNLEIvkllleagadVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDND 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966947269 147 RESALSLACSKGYTDIVKMLLDCGVDVNEYDWNGGTPLLYAVHGNHVKCVKMLLESGADPTIETDSGYNSMDLAVALGYR 226
Cdd:COG0666  186 GETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAA 265

                        170
                 ....*....|....*....
gi 966947269 227 SVQQVIESHLLKLLQNIKE 245
Cdd:COG0666  266 LIVKLLLLALLLLAAALLD 284
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
78-225 5.75e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 97.33  E-value: 5.75e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966947269  78 LLANSLSVHQLAAQGEMLYLATRIEQENVINHTDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQLLGKGRESALSLACSK 157
Cdd:COG0666   18 LLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARN 97

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966947269 158 GYTDIVKMLLDCGVDVNEYDWNGGTPLLYAVHGNHVKCVKMLLESGADPTIETDSGYNSMDLAVALGY 225
Cdd:COG0666   98 GDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165
Ank_2 pfam12796
Ankyrin repeats (3 copies);
118-208 1.36e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.95  E-value: 1.36e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966947269  118 LMWAAAHGQIAVVEFLLQNGADPQLLGKGRESALSLACSKGYTDIVKMLLDCgVDVNEYDwNGGTPLLYAVHGNHVKCVK 197
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|.
gi 966947269  198 MLLESGADPTI 208
Cdd:pfam12796  79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
88-177 2.13e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 69.37  E-value: 2.13e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966947269   88 LAAQGEMLYLATR-IEQENVINHTDEEGFTPLMWAAAHGQIAVVEFLLQNgADPQLLGKGReSALSLACSKGYTDIVKML 166
Cdd:pfam12796   3 LAAKNGNLELVKLlLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGR-TALHYAARSGHLEIVKLL 80

                          90
                  ....*....|.
gi 966947269  167 LDCGVDVNEYD 177
Cdd:pfam12796  81 LEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 107-222 1.07e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 72.78  E-value: 1.07e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966947269 107 INHTDEEGFTPLMWAAAH--GQIAVVEFLLQNGADPQLLGKGRESALSLACSKGYTDI------------------VKML 166
Cdd:PHA03100  99 VNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkilkllidkgvdinaknrVNYL 178

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 966947269 167 LDCGVDVNEYDWNGGTPLLYAVHGNHVKCVKMLLESGADPTIETDSGYNSMDLAVA 222
Cdd:PHA03100 179 LSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAIL 234
Ank_2 pfam12796
Ankyrin repeats (3 copies);
151-228 1.27e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 64.75  E-value: 1.27e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966947269  151 LSLACSKGYTDIVKMLLDCGVDVNEYDWNGGTPLLYAVHGNHVKCVKMLLESGAdpTIETDSGYNSMDLAVALGYRSV 228
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEI 76
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 105-221 1.76e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 66.14  E-value: 1.76e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966947269 105 NVINHTDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQLLGKGRESALSLACSKGYTDIVKML------------------ 166
Cdd:PHA02874  26 NCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLidngvdtsilpipciekd 105

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 966947269 167 -----LDCGVDVNEYDWNGGTPLLYAVHGNHVKCVKMLLESGADPTIETDSGYNSMDLAV 221
Cdd:PHA02874 106 miktiLDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAI 165
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
94-228 1.85e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 62.66  E-value: 1.85e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966947269  94 MLYLATRIEQENVINHTDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQLLGKGRESALSLACSKGYTDIVKMLLDCGVDV 173
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 966947269 174 NEYDWNGGTPLLYAVHGNHVKCVKMLLESGADPTIETDSGYNSMDLAVALGYRSV 228
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI 135
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 112-206 1.46e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 60.39  E-value: 1.46e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966947269 112 EEGFTPLMWAAAHGQIAVVEFLLQNGADPQLLGKGRESALSLACSKGYTDIVKMLLDCGVDVNEYDWNGGTPLLYAVHGN 191
Cdd:PHA02875 100 KDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKG 179

                         90
                 ....*....|....*
gi 966947269 192 HVKCVKMLLESGADP 206
Cdd:PHA02875 180 DIAICKMLLDSGANI 194
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 116-240 1.52e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 60.45  E-value: 1.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966947269 116 TPLMWAAAHGQIAVVEFLLQNGADPQLLGKGRESALSLACSKGYT-----DIVKMLLDCGVDVNEYDWNGGTPLLYAV-- 188
Cdd:PHA03100  37 LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAIsk 116

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 966947269 189 HGNHVKCVKMLLESGADPTIETDSGYNSMDLAVALGYrsvqqvIESHLLKLL 240
Cdd:PHA03100 117 KSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNK------IDLKILKLL 162
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 163-235 5.74e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 58.76  E-value: 5.74e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966947269 163 VKMLLDCGVDVNEYDWNGGTPLLYAVHGNHVKCVKMLLESGADPTIETDSGYNSMDLAVALGYRSVQQVIESH 235
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
Ank_4 pfam13637
Ankyrin repeats (many copies);
147-200 6.42e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.43  E-value: 6.42e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 966947269  147 RESALSLACSKGYTDIVKMLLDCGVDVNEYDWNGGTPLLYAVHGNHVKCVKMLL 200
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 72-180 1.32e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.99  E-value: 1.32e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966947269  72 EVSTTPLLANSLSVH--QLAAQGEMLYLATRIEQENVINHTDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQLLGKGRES 149
Cdd:PTZ00322  71 EEVIDPVVAHMLTVElcQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKT 150

                         90       100       110
                 ....*....|....*....|....*....|.
gi 966947269 150 ALSLACSKGYTDIVKMLLDCGVDVNEYDWNG 180
Cdd:PTZ00322 151 PLELAEENGFREVVQLLSRHSQCHFELGANA 181
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 95-210 2.47e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 56.92  E-value: 2.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966947269  95 LYLATRIEQENV------------INHTDEegFTPLMWAAAHGQIAVVEFLLQNGADPQLLGKGRESALSLACSKGYTDI 162
Cdd:PHA02875 106 LHLATILKKLDImklliargadpdIPNTDK--FSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAI 183

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 966947269 163 VKMLLDCGVDVNEYDWNGGTPLL-YAVHGNHVKCVKMLLESGADPTIET 210
Cdd:PHA02875 184 CKMLLDSGANIDYFGKNGCVAALcYAIENNKIDIVRLFIKRGADCNIMF 232
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 107-228 7.80e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 55.35  E-value: 7.80e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966947269 107 INHTDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQLLGKGRESALSLACSKGYTDIVKMLLDCGVDVNEYDWNGGTPLLY 186
Cdd:PHA02874 117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 966947269 187 AVHGNHVKCVKMLLESGADPTIETDSGYNSMDLAVaLGYRSV 228
Cdd:PHA02874 197 AAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI-IHNRSA 237
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 108-224 7.88e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 55.38  E-value: 7.88e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966947269 108 NHTDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQLLGKGRESALSLACSKGYTDIVKMLLDCGVDVNEYDW-NGGTPLLY 186
Cdd:PHA02875  29 NFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYkDGMTPLHL 108

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 966947269 187 AVHGNHVKCVKMLLESGADPTIETDSGYNSMDLAVALG 224
Cdd:PHA02875 109 ATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMG 146
PHA03095 PHA03095
ankyrin-like protein; Provisional
 107-240 1.12e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 55.03  E-value: 1.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966947269 107 INHTDEEGFTPL---MWAAAHGQIAVVEFLLQNGADPQLLGKGRESAL-SLACSKGYTDIVKMLLDCGVDVNEYDWNGGT 182
Cdd:PHA03095  40 VNFRGEYGKTPLhlyLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLhLYLYNATTLDVIKLLIKAGADVNAKDKVGRT 119

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 966947269 183 PL-LYAVHGN-HVKCVKMLLESGADPTIETDSGYNSMDLAValgyRSVQQVIEshLLKLL 240
Cdd:PHA03095 120 PLhVYLSGFNiNPKVIRLLLRKGADVNALDLYGMTPLAVLL----KSRNANVE--LLRLL 173
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 67-233 1.53e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 54.58  E-value: 1.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966947269  67 KHRGN------EVSTTPLLANSLSvhqlaaqGEMLYLATRIEQENVINHTDEEGFTPLMWAAAHGQIAVVEFLLQNGADP 140
Cdd:PHA02874  22 KNKGNcinisvDETTTPLIDAIRS-------GDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDT 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966947269 141 QLLG---------------------KGRESA--LSLACSKGYTDIVKMLLDCGVDVNEYDWNGGTPLLYAVHGNHVKCVK 197
Cdd:PHA02874  95 SILPipciekdmiktildcgidvniKDAELKtfLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIK 174

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 966947269 198 MLLESGADPTIETDSGYNSMDLAVALG-YRSVQQVIE 233
Cdd:PHA02874 175 LLLEKGAYANVKDNNGESPLHNAAEYGdYACIKLLID 211
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 107-210 1.73e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 54.50  E-value: 1.73e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966947269 107 INHTDEE-GFTPLMWAAAHGQIAVVEFLLQNGADPQLLGKGRESALSLACSKGYTDIVKMLLDCGVDVNEYDWNGGTPLL 185
Cdd:PHA02878 160 INMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLH 239

                         90       100
                 ....*....|....*....|....*.
gi 966947269 186 YAV-HGNHVKCVKMLLESGADPTIET 210
Cdd:PHA02878 240 ISVgYCKDYDILKLLLEHGVDVNAKS 265
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 107-174 2.23e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 53.90  E-value: 2.23e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966947269 107 INHTDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQLLGKGRESALSLACSKGYTDIVKMLLDCGVDVN 174
Cdd:PHA03100 185 INIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 58-211 3.57e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 53.72  E-value: 3.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966947269  58 IKQST---TLTNKHRGNEVSTTPLLANSLSVHQLAAqGEMLYlatrieqENVINHTDEEGFTPLMWAAAHGQIAVVEFLL 134
Cdd:PLN03192 474 LKTSTlieAMQTRQEDNVVILKNFLQHHKELHDLNV-GDLLG-------DNGGEHDDPNMASNLLTVASTGNAALLEELL 545

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966947269 135 QNGADPQLL-GKGReSALSLACSKGYTDIVKMLLDCGVDVNEYDWNGGTPLLYAVHGNHVKCVKML--LESGADPTIETD 211
Cdd:PLN03192 546 KAKLDPDIGdSKGR-TPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILyhFASISDPHAAGD 624
Ank_5 pfam13857
Ankyrin repeats (many copies);
133-187 1.30e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.34  E-value: 1.30e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 966947269  133 LLQNG-ADPQLLGKGRESALSLACSKGYTDIVKMLLDCGVDVNEYDWNGGTPLLYA 187
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
116-167 2.57e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.50  E-value: 2.57e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 966947269  116 TPLMWAAAHGQIAVVEFLLQNGADPQLLGKGRESALSLACSKGYTDIVKMLL 167
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
107-154 4.82e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.80  E-value: 4.82e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 966947269  107 INHTDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQLLGKGRESALSLA 154
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_2 pfam12796
Ankyrin repeats (3 copies);
78-140 1.67e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 45.11  E-value: 1.67e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966947269   78 LLANSLSVHQLAAQGEM-LYLATRIEQENV----INHTD----EEGFTPLMWAAAHGQIAVVEFLLQNGADP 140
Cdd:pfam12796  16 LLENGADANLQDKNGRTaLHLAAKNGHLEIvkllLEHADvnlkDNGRTALHYAARSGHLEIVKLLLEKGADI 87
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 130-210 2.01e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 48.12  E-value: 2.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966947269 130 VEFLLQNGADPQLLGKGRESALSLACSKGYTDIVKMLLDCGVDVNEYDWNGGTPLLYAVHGNHVKCVKMLLESGadPTIE 209
Cdd:PHA03100 175 VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNG--PSIK 252


                 .
gi 966947269 210 T 210
Cdd:PHA03100 253 T 253
Ank_5 pfam13857
Ankyrin repeats (many copies);
166-220 2.93e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.49  E-value: 2.93e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 966947269  166 LLDCG-VDVNEYDWNGGTPLLYAVHGNHVKCVKMLLESGADPTIETDSGYNSMDLA 220
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
101-184 3.70e-06

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 46.87  E-value: 3.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966947269 101 IEQENVINHTDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQLLGKGRESALSLACSKGYTDIVKMLLDCGVDVNEYDWNG 180
Cdd:COG0666  206 LEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285


                 ....
gi 966947269 181 GTPL 184
Cdd:COG0666  286 LTLL 289
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 101-220 5.00e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 46.88  E-value: 5.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966947269 101 IEQENVINHTDEEGFTPLMWAAAHGQIAVVEFLLQNGadpqllgkgreSALSLACSKGYT----------DIVKMLLDcG 170
Cdd:PHA02874 177 LEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHG-----------NHIMNKCKNGFTplhnaiihnrSAIELLIN-N 244

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 966947269 171 VDVNEYDWNGGTPLLYAVHGN-HVKCVKMLLESGADPTIETDSGYNSMDLA 220
Cdd:PHA02874 245 ASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTA 295
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 58-225 9.81e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.21  E-value: 9.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966947269  58 IKQSTTLTNKHRGNEVSTTPLL----ANSLSVHQLAAQGE-MLYLATRIEQENV------------INHTDEEGFTPLMW 120
Cdd:PHA02876 105 IKYASIILNKHKLDEACIHILKeaisGNDIHYDKINESIEyMKLIKERIQQDELliaemlleggadVNAKDIYCITPIHY 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966947269 121 AAAHGQIAVVEFLLQNGADPQLLGKGRESALSLACSKGYTDIVK-----------------------------MLLDCGV 171
Cdd:PHA02876 185 AAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKaiidnrsninkndlsllkairnedletslLLYDAGF 264

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 966947269 172 DVNEYDWNGGTPLLYAVHGNHV-KCVKMLLESGADPTIETDSGYNSMDLAVALGY 225
Cdd:PHA02876 265 SVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAKNGY 319
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 113-140 1.16e-05

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: 41.03  E-value: 1.16e-05
                           10        20
                   ....*....|....*....|....*...
gi 966947269   113 EGFTPLMWAAAHGQIAVVEFLLQNGADP 140
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 129-233 1.43e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 44.81  E-value: 1.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966947269 129 VVEFLLQNGADPQLLGKGRE-SALS--LACSKGYT-DIVKMLLDCGVDVNEYDWNGGTPL-LYAVHGN-HVKCVKMLLES 202
Cdd:PHA02859  68 ILKFLIENGADVNFKTRDNNlSALHhyLSFNKNVEpEILKILIDSGSSITEEDEDGKNLLhMYMCNFNvRINVIKLLIDS 147

                         90       100       110
                 ....*....|....*....|....*....|.
gi 966947269 203 GADPtIETDSGYNSMdLAVALGYRSVQQVIE 233
Cdd:PHA02859 148 GVSF-LNKDFDNNNI-LYSYILFHSDKKIFD 176
Ank_4 pfam13637
Ankyrin repeats (many copies);
85-134 1.78e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.11  E-value: 1.78e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 966947269   85 VHQLAAQGEMLYLATRIEQENVINHTDEEGFTPLMWAAAHGQIAVVEFLL 134
Cdd:pfam13637   5 LHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 126-215 1.90e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 45.12  E-value: 1.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966947269 126 QIAVVEFLLQNGADPQLLG----------KGRESAlslacSKGYTDIVKMLLDCGVDVNEYDWNGGTPL---LYAVHGNH 192
Cdd:PHA02989  49 KIKIVKLLIDNGADVNYKGyietplcavlRNREIT-----SNKIKKIVKLLLKFGADINLKTFNGVSPIvcfIYNSNINN 123

                         90       100
                 ....*....|....*....|....
gi 966947269 193 VKCVKMLLESGAD-PTIETDSGYN 215
Cdd:PHA02989 124 CDMLRFLLSKGINvNDVKNSRGYN 147
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 113-140 2.38e-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: 40.35  E-value: 2.38e-05
                          10        20
                  ....*....|....*....|....*....
gi 966947269  113 EGFTPLMWAAAH-GQIAVVEFLLQNGADP 140
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADV 29
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 113-140 2.68e-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: 39.93  E-value: 2.68e-05
                          10        20
                  ....*....|....*....|....*...
gi 966947269  113 EGFTPLMWAAAHGQIAVVEFLLQNGADP 140
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
PHA03095 PHA03095
ankyrin-like protein; Provisional
 107-167 2.92e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 44.63  E-value: 2.92e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966947269 107 INHTDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQLLGKGRESALSLACSKGYTDIVKMLL 167
Cdd:PHA03095 250 INARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
PHA02798 PHA02798
ankyrin-like protein; Provisional
 129-240 5.39e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 43.67  E-value: 5.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966947269 129 VVEFLLQNGADpqLLGKGRESALSLaCS--------KGYTDIVKMLLDCGVDVNEYDWNGGTPLLYAVHG---NHVKCVK 197
Cdd:PHA02798  53 IVKLFINLGAN--VNGLDNEYSTPL-CTilsnikdyKHMLDIVKILIENGADINKKNSDGETPLYCLLSNgyiNNLEILL 129

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 966947269 198 MLLESGADPTIETDSGYNSMDLAVALGYRsvqqvIESHLLKLL 240
Cdd:PHA02798 130 FMIENGADTTLLDKDGFTMLQVYLQSNHH-----IDIEIIKLL 167
PHA02792 PHA02792
ankyrin-like protein; Provisional
 129-243 5.58e-05

ankyrin-like protein; Provisional


Pssm-ID: 165155 [Multi-domain]  Cd Length: 631  Bit Score: 43.78  E-value: 5.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966947269 129 VVEFLLQNGAD---------------PQLLGKGRESALSLACSKGYTDivkmlldcgvDVNEYDWNGGTPLLYAVHGNHV 193
Cdd:PHA02792 354 VVEYILKNGNVvvedddniinimplfPTLSIHESDVLSILKLCKPYID----------DINKIDKHGRSILYYCIESHSV 423

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 966947269 194 KCVKMLLESGADPTIETDSGYNSMDLAVALGYRSVQQVIESHlLKLLQNI 243
Cdd:PHA02792 424 SLVEWLIDNGADINITTKYGSTCIGICVILAHACIPEIAELY-IKILEII 472
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 179-211 8.45e-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: 38.81  E-value: 8.45e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 966947269  179 NGGTPLLYAV-HGNHVKCVKMLLESGADPTIETD 211
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 107-233 9.71e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 43.13  E-value: 9.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966947269 107 INHTDEEGFTPLMWAAAHG-QIAVVEFLLQNGADPQLLGKGRESALSLACS-KGYTDIVKMLLDCGVDVNEYDWNGGTPL 184
Cdd:PHA02876 300 VNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPI 379

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 966947269 185 LYAVHGNHVKCVKMLLESGADptIETDSGYNSMDLAVAL----GYRSVQQVIE 233
Cdd:PHA02876 380 HYAAVRNNVVIINTLLDYGAD--IEALSQKIGTALHFALcgtnPYMSVKTLID 430
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 116-232 1.27e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 42.67  E-value: 1.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966947269 116 TPLMWAAAHGQIAVVEFLLQNG--ADPQLLGKGReSALSLACSKGYTDIVKMLLDCGVDVNEYDWNGGTPLLYAVHGNHV 193
Cdd:PHA02875  70 SELHDAVEEGDVKAVEELLDLGkfADDVFYKDGM-TPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI 148

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 966947269 194 KCVKMLLESGADPTIETDSGYNSMDLAVALGYRSVQQVI 232
Cdd:PHA02875 149 KGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKML 187
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 107-232 1.31e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 42.93  E-value: 1.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966947269 107 INHTDEEGFTPlMW---AAAHGQIAVVEFLLQNGADPQLLGkgreSALSLACSKGYTDIVKMLLDCGVDVNEYDWNGGTP 183
Cdd:PLN03192 584 VHIRDANGNTA-LWnaiSAKHHKIFRILYHFASISDPHAAG----DLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATA 658

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 966947269 184 LLYAVHGNHVKCVKMLLESGADPT-IETDSGYNSMDLAVALGYRSVQQVI 232
Cdd:PLN03192 659 LQVAMAEDHVDMVRLLIMNGADVDkANTDDDFSPTELRELLQKRELGHSI 708
PHA02791 PHA02791
ankyrin-like protein; Provisional
 111-201 1.43e-04

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 41.95  E-value: 1.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966947269 111 DEEGFTPLMWAAAHGQIAVVEFLLQNGADPQLLGKgrESALSLACSKGYTDIVKMLLDCGVDVNEYDWNGGTPLLYAVHG 190
Cdd:PHA02791  27 DVHGHSALYYAIADNNVRLVCTLLNAGALKNLLEN--EFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDS 104

                         90
                 ....*....|.
gi 966947269 191 NHVKCVKMLLE 201
Cdd:PHA02791 105 GNMQTVKLFVK 115
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 179-208 3.16e-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: 37.18  E-value: 3.16e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 966947269   179 NGGTPLLYAVHGNHVKCVKMLLESGADPTI 208
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 113-184 4.36e-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: 4.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966947269 113 EGFTPLMWAAAHGQIAVVEFLLQNGADPQ---------LLGKGR-----ESALSLACSKGYTDIVKMLLDCGVDVNEYDW 178
Cdd:cd22192   88 QGETALHIAVVNQNLNLVRELIARGADVVspratgtffRPGPKNliyygEHPLSFAACVGNEEIVRLLIEHGADIRAQDS 167


                 ....*.
gi 966947269 179 NGGTPL 184
Cdd:cd22192  168 LGNTVL 173
PHA02798 PHA02798
ankyrin-like protein; Provisional
 127-218 6.97e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 40.20  E-value: 6.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966947269 127 IAVVEFLLQNGADPQLLGKGRESALSLACSKGYT---DIVKMLLDCGVDVNEYDWNGGTPL-LYAVHGNHV--KCVKMLL 200
Cdd:PHA02798  89 LDIVKILIENGADINKKNSDGETPLYCLLSNGYInnlEILLFMIENGADTTLLDKDGFTMLqVYLQSNHHIdiEIIKLLL 168

                         90
                 ....*....|....*....
gi 966947269 201 ESGAD-PTIETDSGYNSMD 218
Cdd:PHA02798 169 EKGVDiNTHNNKEKYDTLH 187
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 116-205 7.83e-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: 40.38  E-value: 7.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966947269 116 TPLMWAAAHGQI-AVVEFLLQNGADPQLLGKGRESALSLACSKGYTDIVKMLLDCGVD-VNE------YDwnGGTPLLYA 187
Cdd:cd22192   19 SPLLLAAKENDVqAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEpmtsdlYQ--GETALHIA 96

                         90
                 ....*....|....*...
gi 966947269 188 VHGNHVKCVKMLLESGAD 205
Cdd:cd22192   97 VVNQNLNLVRELIARGAD 114
PHA03095 PHA03095
ankyrin-like protein; Provisional
 107-222 8.95e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 40.01  E-value: 8.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966947269 107 INHTDEEGFTPL------MWAAAhgqiAVVEFLLQNGADPQ--------------------------LLGKG-------- 146
Cdd:PHA03095 110 VNAKDKVGRTPLhvylsgFNINP----KVIRLLLRKGADVNaldlygmtplavllksrnanvellrlLIDAGadvyavdd 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966947269 147 -RESAL-SLACS-KGYTDIVKMLLD------------------------C-----------GVDVNEYDWNGGTPLLYA- 187
Cdd:PHA03095 186 rFRSLLhHHLQSfKPRARIVRELIRagcdpaatdmlgntplhsmatgssCkrslvlplliaGISINARNRYGQTPLHYAa 265

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 966947269 188 VHGNHVKCVKmLLESGADPTIETDSGYNSMDLAVA 222
Cdd:PHA03095 266 VFNNPRACRR-LIALGADINAVSSDGNTPLSLMVR 299
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 89-205 9.86e-04

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: 40.06  E-value: 9.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966947269   89 AAQGEMLYLATRIEQENV---INHTDEEGFTPLMWAAAHGQ-IAVVEFLLQNGADPQLlGKgresALSLACSKGYTDIVK 164
Cdd:TIGR00870  24 AAERGDLASVYRDLEEPKklnINCPDRLGRSALFVAAIENEnLELTELLLNLSCRGAV-GD----TLLHAISLEYVDAVE 98

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 966947269  165 MLL----------DCGVDVNEYDWN----GGTPLLYAVHGNHVKCVKMLLESGAD 205
Cdd:TIGR00870  99 AILlhllaafrksGPLELANDQYTSeftpGITALHLAAHRQNYEIVKLLLERGAS 153
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 129-240 9.97e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 39.86  E-value: 9.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966947269 129 VVEFLLQNGADPQLLGKGR-ESALSLACSKGYTDIVKMLLDCGVDVNEYDWNGGTPLLYAVHGNHVKCVKMLLESGAdpT 207
Cdd:PHA02878 149 ITKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA--S 226

                         90       100       110
                 ....*....|....*....|....*....|...
gi 966947269 208 IETDSGYNSMDLAVALGYrsvqqVIESHLLKLL 240
Cdd:PHA02878 227 TDARDKCGNTPLHISVGY-----CKDYDILKLL 254
Ank_4 pfam13637
Ankyrin repeats (many copies);
180-228 1.25e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.10  E-value: 1.25e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 966947269  180 GGTPLLYAVHGNHVKCVKMLLESGADPTIETDSGYNSMDLAVALGYRSV 228
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEV 49
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 148-175 1.43e-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: 35.31  E-value: 1.43e-03
                          10        20
                  ....*....|....*....|....*...
gi 966947269  148 ESALSLACSKGYTDIVKMLLDCGVDVNE 175
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 28-205 2.22e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 38.89  E-value: 2.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966947269  28 YAECNIHTSPSPGIQVrhvyTPSTTKHFSPIKQSTTLtNKHRGNEVSTTPLLAN--------SLSVHQLAAQGEMLYLAT 99
Cdd:PHA02876 319 YDTENIRTLIMLGADV----NAADRLYITPLHQASTL-DRNKDIVITLLELGANvnardycdKTPIHYAAVRNNVVIINT 393

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966947269 100 RIEQENVINHTDEEGFTPLMWA-AAHGQIAVVEFLLQNGADPQLLGKGRESALSLACSKG-YTDIVKMLLDCGVDVNEYD 177
Cdd:PHA02876 394 LLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAIN 473

                        170       180
                 ....*....|....*....|....*...
gi 966947269 178 WNGGTPLLYAVHGNHVkcVKMLLESGAD 205
Cdd:PHA02876 474 IQNQYPLLIALEYHGI--VNILLHYGAE 499
PHA02795 PHA02795
ankyrin-like protein; Provisional
 161-240 2.36e-03

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 38.82  E-value: 2.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966947269 161 DIVKMLLDCGVDVNEYDWNGGTPLLYAVHGNHVKCVKMLLESGADPTIETDSGYNSMDLAVALGYRSVQQVIESHLLKLL 240
Cdd:PHA02795 202 EIYKLCIPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRGSVIARRETHLKILEIL 281
PHA02798 PHA02798
ankyrin-like protein; Provisional
 101-174 2.42e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 38.66  E-value: 2.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966947269 101 IEQENVINHTDEEGFTPLMWAAAHGQIAVVEFLL---QNGADPQLLGKGRESALSLACSKGYT---DIVKMLLDCGVDVN 174
Cdd:PHA02798  96 IENGADINKKNSDGETPLYCLLSNGYINNLEILLfmiENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDIN 175
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 179-208 3.86e-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: 34.16  E-value: 3.86e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 966947269  179 NGGTPLLYAVHGNHVKCVKMLLESGADPTI 208
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02798 PHA02798
ankyrin-like protein; Provisional
 111-213 4.49e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 37.89  E-value: 4.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966947269 111 DEEGFTPL---MWAAAHGQIAVVEFLLQNGADPQLLGKgRESALSLACSKGYT------DIVKMLLDCG----------- 170
Cdd:PHA02798 142 DKDGFTMLqvyLQSNHHIDIEIIKLLLEKGVDINTHNN-KEKYDTLHCYFKYNidridaDILKLFVDNGfiinkenkshk 220

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966947269 171 ----------------------------VDVNEYDWNGGTPLLYAVHGNHVKCVKMLLESGADPTIETDSG 213
Cdd:PHA02798 221 kkfmeylnsllydnkrfkknildfifsyIDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELG 291
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 149-175 5.67e-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: 5.67e-03
                           10        20
                   ....*....|....*....|....*..
gi 966947269   149 SALSLACSKGYTDIVKMLLDCGVDVNE 175
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 129-232 6.36e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 37.27  E-value: 6.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966947269 129 VVEFLLQNGADPQLLGKGRESA----LSLACSKGYTDIVKMLLDCGVDVNEY-DWNGGTPLLYAVHGNHVKCVKMLLESG 203
Cdd:PHA02884  48 IIDAILKLGADPEAPFPLSENSktnpLIYAIDCDNDDAAKLLIRYGADVNRYaEEAKITPLYISVLHGCLKCLEILLSYG 127

                         90       100
                 ....*....|....*....|....*....
gi 966947269 204 ADPTIETDSGYNSMDLAVALGYRSVQQVI 232
Cdd:PHA02884 128 ADINIQTNDMVTPIELALMICNNFLAFMI 156
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 148-177 6.37e-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: 33.42  E-value: 6.37e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 966947269  148 ESALSLACSK-GYTDIVKMLLDCGVDVNEYD 177
Cdd:pfam00023   3 NTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
PHA03095 PHA03095
ankyrin-like protein; Provisional
 153-219 6.37e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 37.31  E-value: 6.37e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966947269 153 LACSKGYTDIVKMLLDCGVDVNEYDWNGGTPLLYAVHGNHVKC---VKMLLESGADPTIETDSGYNSMDL 219
Cdd:PHA03095  20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLHL 89
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 107-214 9.87e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 36.78  E-value: 9.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966947269 107 INHTDEEGFTPLMWAAAH-GQIAVVEFLLQNGADPQLLGKGRE-SALSLACSKgyTDIVKMLLDCGVDVNEYDWNGGTPL 184
Cdd:PHA02878 227 TDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYILGlTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPL 304

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 966947269 185 LYAVHGNH-VKCVKML-----LESGADPTIETDSGY 214
Cdd:PHA02878 305 SSAVKQYLcINIGRILisnicLLKRIKPDIKNSEGF 340
 
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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