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Conserved domains on  [gi|1034574313|ref|XP_016873430|]
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ankyrin repeat domain-containing protein 49 isoform X1 [Homo sapiens]

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];
77-218 1.01e-36

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 130.84  E-value: 1.01e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574313  77 LLLWAAEKNRLTTVRRLLSEKAtHVNTRDEDEYTPLHRAAYSGHLDIVQELIAQGADVHAVTVDGWTPLHSACKWNNTRV 156
Cdd:COG0666    90 LLHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEI 168

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034574313 157 ASFLLQHDADINAQTKGLLTPLHLAAGNRDsKDTLELLLmNRYVKPGLKNNLEETAFDIARR 218
Cdd:COG0666   169 VKLLLEAGADVNARDNDGETPLHLAAENGH-LEIVKLLL-EAGADVNAKDNDGKTALDLAAE 228
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
77-218 1.01e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 130.84  E-value: 1.01e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574313  77 LLLWAAEKNRLTTVRRLLSEKAtHVNTRDEDEYTPLHRAAYSGHLDIVQELIAQGADVHAVTVDGWTPLHSACKWNNTRV 156
Cdd:COG0666    90 LLHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEI 168

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034574313 157 ASFLLQHDADINAQTKGLLTPLHLAAGNRDsKDTLELLLmNRYVKPGLKNNLEETAFDIARR 218
Cdd:COG0666   169 VKLLLEAGADVNARDNDGETPLHLAAENGH-LEIVKLLL-EAGADVNAKDNDGKTALDLAAE 228
Ank_2 pfam12796
Ankyrin repeats (3 copies);
112-197 1.82e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.17  E-value: 1.82e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574313 112 LHRAAYSGHLDIVQELIAQGADVHAVTVDGWTPLHSACKWNNTRVASFLLQHdADINAQTKGlLTPLHLAAGNRdSKDTL 191
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG-RTALHYAARSG-HLEIV 77


                  ....*.
gi 1034574313 192 ELLLMN 197
Cdd:pfam12796  78 KLLLEK 83
PHA03095 PHA03095
ankyrin-like protein; Provisional
 82-215 6.83e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 76.22  E-value: 6.83e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574313  82 AEKNRLTTVRRLLSEKAThVNTRDEDEYTPLH---RAAYSGHLDIVQELIAQGADVHAVTVDGWTPLHSACKWNNT-RVA 157
Cdd:PHA03095   22 ASNVTVEEVRRLLAAGAD-VNFRGEYGKTPLHlylHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVI 100

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034574313 158 SFLLQHDADINAQTKGLLTPLHL-AAGNRDSKDTLELLLmNRYVKPGLKNNLEETAFDI 215
Cdd:PHA03095  101 KLLIKAGADVNAKDKVGRTPLHVyLSGFNINPKVIRLLL-RKGADVNALDLYGMTPLAV 158
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 60-180 3.66e-06

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: 47.31  E-value: 3.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574313  60 EEWYRLQEKKMEKDPsrlLLWAAEKNRLTTVRRLLS-------------EKATHV---NTRDE----------------- 106
Cdd:cd22192     6 DELHLLQQKRISESP---LLLAAKENDVQAIKKLLKcpscdlfqrgalgETALHVaalYDNLEaavvlmeaapelvnepm 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574313 107 --DEY---TPLHRAAYSGHLDIVQELIAQGADV--------------HAVTVDGWTPLHSACKWNNTRVASFLLQHDADI 167
Cdd:cd22192    83 tsDLYqgeTALHIAVVNQNLNLVRELIARGADVvspratgtffrpgpKNLIYYGEHPLSFAACVGNEEIVRLLIEHGADI 162

                         170
                  ....*....|...
gi 1034574313 168 NAQTKGLLTPLHL 180
Cdd:cd22192   163 RAQDSLGNTVLHI 175
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 140-169 4.74e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.19  E-value: 4.74e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 1034574313  140 DGWTPLHSACKWNNTRVASFLLQHDADINA 169
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 100-199 3.91e-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: 38.14  E-value: 3.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574313 100 HVNTRDEDEY----TPLHRAAYSGHLDIVQELIAQGADVHA-------VTVDGWT-------PLHSACKWNNTRVASFLL 161
Cdd:TIGR00870 116 LANDQYTSEFtpgiTALHLAAHRQNYEIVKLLLERGASVPAracgdffVKSQGVDsfyhgesPLNAAACLGSPSIVALLS 195

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1034574313 162 QHDADINAQTKGLLTPLHLAAGNRDSKDTLELLLMNRY 199
Cdd:TIGR00870 196 EDPADILTADSLGNTLLHLLVMENEFKAEYEELSCQMY 233
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
77-218 1.01e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 130.84  E-value: 1.01e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574313  77 LLLWAAEKNRLTTVRRLLSEKAtHVNTRDEDEYTPLHRAAYSGHLDIVQELIAQGADVHAVTVDGWTPLHSACKWNNTRV 156
Cdd:COG0666    90 LLHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEI 168

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034574313 157 ASFLLQHDADINAQTKGLLTPLHLAAGNRDsKDTLELLLmNRYVKPGLKNNLEETAFDIARR 218
Cdd:COG0666   169 VKLLLEAGADVNARDNDGETPLHLAAENGH-LEIVKLLL-EAGADVNAKDNDGKTALDLAAE 228
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
77-218 9.06e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 115.05  E-value: 9.06e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574313  77 LLLWAAEKNRLTTVRRLLSEKAtHVNTRDEDEYTPLHRAAYSGHLDIVQELIAQGADVHAVTVDGWTPLHSACKWNNTRV 156
Cdd:COG0666   123 PLHLAAYNGNLEIVKLLLEAGA-DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEI 201

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034574313 157 ASFLLQHDADINAQTKGLLTPLHLAAGNRDSKDTLELLLMNRYVKPGLKNNLEETAFDIARR 218
Cdd:COG0666   202 VKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAG 263
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
72-216 1.97e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 111.58  E-value: 1.97e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574313  72 KDPSRLLLWAAEKNRLTTVRRLLSEKATHVNTRDEDEYTPLHRAAYSGHLDIVQELIAQGADVHAVTVDGWTPLHSACKW 151
Cdd:COG0666    51 DALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYN 130

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034574313 152 NNTRVASFLLQHDADINAQTKGLLTPLHLAAGNRDsKDTLELLLmNRYVKPGLKNNLEETAFDIA 216
Cdd:COG0666   131 GNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN-LEIVKLLL-EAGADVNARDNDGETPLHLA 193
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
77-209 1.24e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 98.87  E-value: 1.24e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574313  77 LLLWAAEKNRLTTVRRLLSEKAtHVNTRDEDEYTPLHRAAYSGHLDIVQELIAQGADVHAVTVDGWTPLHSACKWNNTRV 156
Cdd:COG0666   156 PLHLAAANGNLEIVKLLLEAGA-DVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI 234

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1034574313 157 ASFLLQHDADINAQTKGLLTPLHLAAGNRDSKDTLELLLMNRYVKPGLKNNLE 209
Cdd:COG0666   235 VKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
Ank_2 pfam12796
Ankyrin repeats (3 copies);
112-197 1.82e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.17  E-value: 1.82e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574313 112 LHRAAYSGHLDIVQELIAQGADVHAVTVDGWTPLHSACKWNNTRVASFLLQHdADINAQTKGlLTPLHLAAGNRdSKDTL 191
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG-RTALHYAARSG-HLEIV 77


                  ....*.
gi 1034574313 192 ELLLMN 197
Cdd:pfam12796  78 KLLLEK 83
Ank_2 pfam12796
Ankyrin repeats (3 copies);
78-170 3.99e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.40  E-value: 3.99e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574313  78 LLWAAEKNRLTTVRRLLSEKAtHVNTRDEDEYTPLHRAAYSGHLDIVQELIAQgADVhAVTVDGWTPLHSACKWNNTRVA 157
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGA-DANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADV-NLKDNGRTALHYAARSGHLEIV 77

                          90
                  ....*....|...
gi 1034574313 158 SFLLQHDADINAQ 170
Cdd:pfam12796  78 KLLLEKGADINVK 90
PHA03095 PHA03095
ankyrin-like protein; Provisional
 82-215 6.83e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 76.22  E-value: 6.83e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574313  82 AEKNRLTTVRRLLSEKAThVNTRDEDEYTPLH---RAAYSGHLDIVQELIAQGADVHAVTVDGWTPLHSACKWNNT-RVA 157
Cdd:PHA03095   22 ASNVTVEEVRRLLAAGAD-VNFRGEYGKTPLHlylHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVI 100

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034574313 158 SFLLQHDADINAQTKGLLTPLHL-AAGNRDSKDTLELLLmNRYVKPGLKNNLEETAFDI 215
Cdd:PHA03095  101 KLLIKAGADVNAKDKVGRTPLHVyLSGFNINPKVIRLLL-RKGADVNALDLYGMTPLAV 158
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
56-216 1.77e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 73.83  E-value: 1.77e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574313  56 DDKNEEWYRLQEKKMEKDPSRLLLWAAEKNRLTTVRRLLSEKATHVNTRDEDEYTPLHRAAYSGHLDIVQELIAQGADVH 135
Cdd:COG0666     2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574313 136 AVTVDGWTPLHSACKWNNTRVASFLLQHDADINAQTKGLLTPLHLAAGNRDsKDTLELLLmNRYVKPGLKNNLEETAFDI 215
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGN-LEIVKLLL-EAGADVNAQDNDGNTPLHL 159


                  .
gi 1034574313 216 A 216
Cdd:COG0666   160 A 160
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 85-169 3.58e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 73.93  E-value: 3.58e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574313  85 NRLTTVRRLLSeKATHVNTRDEDEYTPLHRAAYSGHLDIVQELIAQGADVHAVTVDGWTPLHSACKWNNTRVASFLLQHD 164
Cdd:PHA03100  170 NAKNRVNYLLS-YGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNG 248


                  ....*
gi 1034574313 165 ADINA 169
Cdd:PHA03100  249 PSIKT 253
Ank_4 pfam13637
Ankyrin repeats (many copies);
108-161 3.50e-14

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 64.99  E-value: 3.50e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1034574313 108 EYTPLHRAAYSGHLDIVQELIAQGADVHAVTVDGWTPLHSACKWNNTRVASFLL 161
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 72-195 2.92e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 65.43  E-value: 2.92e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574313  72 KDPSRLLLWAAEKNRLTTVRRLLsEKATHVNTRDEDEYTPLHRAAYSGH-LDIVQELIAQGADVHAVTVDGWTPLHSAC- 149
Cdd:PHA03095   48 KTPLHLYLHYSSEKVKDIVRLLL-EAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGADVNAKDKVGRTPLHVYLs 126

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1034574313 150 -KWNNTRVASFLLQHDADINAQTKGLLTPLHLAAGNRD-SKDTLELLL 195
Cdd:PHA03095  127 gFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNaNVELLRLLI 174
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 77-225 1.72e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 63.06  E-value: 1.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574313  77 LLLWAAEKNRLTTVRRLLSEKAThVNTRDEDEYTPLHRAAYSGHLDIVQELIAQGADVHAVTVDGWTPLHSACKWNNTRV 156
Cdd:PHA02874  127 FLHYAIKKGDLESIKMLFEYGAD-VNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYAC 205

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034574313 157 ASFLLQHDADINAQTKGLLTPLHLAagnrdskdtlelLLMNRYVKPGLKNNLEETAFDIARRTSIYHYL 225
Cdd:PHA02874  206 IKLLIDHGNHIMNKCKNGFTPLHNA------------IIHNRSAIELLINNASINDQDIDGSTPLHHAI 262
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 72-199 6.64e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 61.22  E-value: 6.64e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574313  72 KDPSRLLLWAAEKNRLTTVRRLLsEKATHVNTRDEDEYTPLHRAAYSGH-----LDIVQELIAQGADVHAVTVDGWTPLH 146
Cdd:PHA03100   33 KKPVLPLYLAKEARNIDVVKILL-DNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITPLL 111

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034574313 147 SA--CKWNNTRVASFLLQHDADINAQTKGLLTPLHLAA-GNRDSKDTLELLLMNRY 199
Cdd:PHA03100  112 YAisKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLeSNKIDLKILKLLIDKGV 167
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 82-216 1.25e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 60.75  E-value: 1.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574313  82 AEKNRLTTVRRLLSEKATHVNTRDEDEYTPLHRAAYSGHLDIVQELIAQGADVHAVTVDGWTPLHSACKWNntRVASFLL 161
Cdd:PHA02874  164 AIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHN--RSAIELL 241

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1034574313 162 QHDADINAQTKGLLTPLHLAAGNRDSKDTLELLLMNRyVKPGLKNNLEETAFDIA 216
Cdd:PHA02874  242 INNASINDQDIDGSTPLHHAINPPCDIDIIDILLYHK-ADISIKDNKGENPIDTA 295
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
78-178 1.34e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 59.97  E-value: 1.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574313  78 LLWAAEKNRLTTVRRLLSEKAtHVNTRDEDEYTPLHRAAYSGHLDIVQELIAQGADVHAVTVDGWTPLHSACKWNNTRVA 157
Cdd:COG0666   190 LHLAAENGHLEIVKLLLEAGA-DVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIV 268

                          90       100
                  ....*....|....*....|.
gi 1034574313 158 SFLLQHDADINAQTKGLLTPL 178
Cdd:COG0666   269 KLLLLALLLLAAALLDLLTLL 289
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 94-197 1.81e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 60.46  E-value: 1.81e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574313  94 LSEKATHVNTRDEDEYTPLHRAAYSGHLDIVQELIAQGADVHAVTVDGWTPLHSA-CKWNNTRVASFLLQHDADINAQTK 172
Cdd:PHA02876  361 LLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNK 440

                          90       100
                  ....*....|....*....|....*
gi 1034574313 173 GLLTPLHLAAGNRDSKDTLELLLMN 197
Cdd:PHA02876  441 DLSTPLHYACKKNCKLDVIEMLLDN 465
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 88-195 3.27e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 59.51  E-value: 3.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574313  88 TTVRRLLSEKATHVNTRDEDE-YTPLHRAAYSGHLDIVQELIAQGADVHAVTVDGWTPLHSACKWNNTRVASFLLQHDAD 166
Cdd:PHA02878  147 AEITKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS 226

                          90       100
                  ....*....|....*....|....*....
gi 1034574313 167 INAQTKGLLTPLHLAAGNRDSKDTLELLL 195
Cdd:PHA02878  227 TDARDKCGNTPLHISVGYCKDYDILKLLL 255
Ank_4 pfam13637
Ankyrin repeats (many copies);
75-128 5.39e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.43  E-value: 5.39e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1034574313  75 SRLLLWAAEKNRLTTVRRLLsEKATHVNTRDEDEYTPLHRAAYSGHLDIVQELI 128
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLL-EKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 68-195 5.67e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 58.74  E-value: 5.67e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574313  68 KKMEKDPSRLLLWAAEKNRLTTVRRLLSEKATHVNTRDEDEYTPLHRAAYSGHLDIVQELIAQGADVHAVTVDGWTPLH- 146
Cdd:PHA02878  161 NMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHi 240

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1034574313 147 SACKWNNTRVASFLLQHDADINAQTKGL-LTPLHLAAgnrDSKDTLELLL 195
Cdd:PHA02878  241 SVGYCKDYDILKLLLEHGVDVNAKSYILgLTALHSSI---KSERKLKLLL 287
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 77-198 6.19e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 58.52  E-value: 6.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574313  77 LLLWAAEKNRLTTVRRLLSEKATHVNTRDEDEYTPLHRAAYSGH--LDIVQELIAQGADVHAVT-VD------------- 140
Cdd:PHA03100  110 LLYAISKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKNrVNyllsygvpinikd 189

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574313 141 --GWTPLHSACKWNNTRVASFLLQHDADINAQTKGLLTPLHLAAGNRDsKDTLELLLMNR 198
Cdd:PHA03100  190 vyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNN-KEIFKLLLNNG 248
Ank_4 pfam13637
Ankyrin repeats (many copies);
141-195 1.03e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.97  E-value: 1.03e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1034574313 141 GWTPLHSACKWNNTRVASFLLQHDADINAQTKGLLTPLHLAAGNRDsKDTLELLL 195
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGN-VEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 89-197 1.31e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 54.58  E-value: 1.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574313  89 TVRRLLsEKATHVNTRDEDEYTPLHRAAYSGHLDIVQELIAQGADVHAVTVDGWTPLHSACKWNNTRVASFLLQHDADIN 168
Cdd:PHA02874  106 MIKTIL-DCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184

                          90       100
                  ....*....|....*....|....*....
gi 1034574313 169 AQTKGLLTPLHLAAGNRDSKdTLELLLMN 197
Cdd:PHA02874  185 VKDNNGESPLHNAAEYGDYA-CIKLLIDH 212
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 79-208 1.62e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 54.50  E-value: 1.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574313  79 LWAAEKNRLTTVRRLLSEKATHVNTRDEDEYTPLHRA-AYSGHLDIVQELIAQGADVHA-VTVDGWTPLHSACKwnNTRV 156
Cdd:PHA02878  205 LHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAkSYILGLTALHSSIK--SERK 282

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034574313 157 ASFLLQHDADINAQTKGLLTPLHLAAGNRDSKDTLELLLMN----RYVKPGLKNNL 208
Cdd:PHA02878  283 LKLLLEYGADINSLNSYKLTPLSSAVKQYLCINIGRILISNicllKRIKPDIKNSE 338
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 92-163 2.28e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.13  E-value: 2.28e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034574313  92 RLLSEKATHVNTRDEDEYTPLHRAAYSGHLDIVQELIAQGADVHAVTVDGWTPLHSACKWNNTRVASFLLQH 163
Cdd:PTZ00322   99 RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 77-195 2.93e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 53.91  E-value: 2.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574313  77 LLLWAAEKNRLTTVRRLLSEKATHVNTRDEDEYTPLHRAAYSGHLD-IVQELIAQGADVHAVTVDGWTPLHSACKWN-NT 154
Cdd:PHA02876  242 LSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGyDT 321

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1034574313 155 RVASFLLQHDADINAQTKGLLTPLHLAAGNRDSKDTLELLL 195
Cdd:PHA02876  322 ENIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIVITLL 362
PHA03095 PHA03095
ankyrin-like protein; Provisional
 88-186 2.94e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 53.49  E-value: 2.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574313  88 TTVRRLLSEKATHVNTRDEDEYTPLHRAAY--SGHLDIVQELIAQGADVHAVTVDGWTPLHSACKWNNTRVASFLLQHDA 165
Cdd:PHA03095  202 ARIVRELIRAGCDPAATDMLGNTPLHSMATgsSCKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGA 281

                          90       100
                  ....*....|....*....|.
gi 1034574313 166 DINAQTKGLLTPLHLAAGNRD 186
Cdd:PHA03095  282 DINAVSSDGNTPLSLMVRNNN 302
Ank_5 pfam13857
Ankyrin repeats (many copies);
93-148 3.41e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.88  E-value: 3.41e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034574313  93 LLSEKATHVNTRDEDEYTPLHRAAYSGHLDIVQELIAQGADVHAVTVDGWTPLHSA 148
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 82-198 4.16e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 53.07  E-value: 4.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574313  82 AEKNRLTTVRRLLSEKATHVNTRDEDEYTPLHRAAYSGHLDIVQELIAQGADVHAVTV-DGWTPLHSACKWNNTRVASFL 160
Cdd:PHA02875   42 AMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYkDGMTPLHLATILKKLDIMKLL 121

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1034574313 161 LQHDADINAQTKGLLTPLHLAAGNRDSKDTlELLLMNR 198
Cdd:PHA02875  122 IARGADPDIPNTDKFSPLHLAVMMGDIKGI-ELLIDHK 158
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 83-198 1.49e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 51.20  E-value: 1.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574313  83 EKNRLTTV--RRLLSEKATHVNTRDEDEYTPLHRAAYSGHLDIVQELIAQGADVHAVTVDGWTPLHSACKW-----NNTR 155
Cdd:PHA03100    8 TKSRIIKVknIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIkynltDVKE 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1034574313 156 VASFLLQHDADINAQTKGLLTPLHLAAGNR-DSKDTLELLLMNR 198
Cdd:PHA03100   88 IVKLLLEYGANVNAPDNNGITPLLYAISKKsNSYSIVEYLLDNG 131
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 24-193 7.53e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 49.29  E-value: 7.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574313  24 FNQLELLETHGHLIPTGtqslwVGNSDEDEEQDDKNEEWYRLQEKKMEKDPSRlllwaaeknrlttVRRLLSEKATHVNT 103
Cdd:PHA02876  112 LNKHKLDEACIHILKEA-----ISGNDIHYDKINESIEYMKLIKERIQQDELL-------------IAEMLLEGGADVNA 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574313 104 RDEDEYTPLHRAAYSGHLDIVQELIAQGADVHAVTVDGWTPLHSACKWNNTRVASFLLQHDADINAQTKGLLTplhlAAG 183
Cdd:PHA02876  174 KDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNDLSLLK----AIR 249

                         170
                  ....*....|
gi 1034574313 184 NRDSKDTLEL 193
Cdd:PHA02876  250 NEDLETSLLL 259
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 81-186 1.03e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 48.83  E-value: 1.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574313  81 AAEKNRLTTVRRLLSEKATHVNTRDEDEYTPLHRAAYSGHLDIVQELIAQGADVHAVTVDGWTPLHSACKWNNTRVASFL 160
Cdd:PHA02875   75 AVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELL 154

                          90       100
                  ....*....|....*....|....*.
gi 1034574313 161 LQHDADINAQTKGLLTPLHLAAGNRD 186
Cdd:PHA02875  155 IDHKACLDIEDCCGCTPLIIAMAKGD 180
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 140-172 1.13e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 43.82  E-value: 1.13e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1034574313 140 DGWTPLHSAC-KWNNTRVASFLLQHDADINAQTK 172
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 78-175 1.38e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 48.51  E-value: 1.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574313  78 LLWAAEKNRLTTVRRLLsEKATHVNTRDEDEYTPLHRAAYSGHLDIVQELIAQGADVhavtvdgwtplhsackwnNTRVA 157
Cdd:PHA03100  196 LHYAVYNNNPEFVKYLL-DLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSI------------------KTIIE 256

                          90
                  ....*....|....*...
gi 1034574313 158 SFLLQHDADINAQTKGLL 175
Cdd:PHA03100  257 TLLYFKDKDLNTITKIKM 274
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 72-181 1.90e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.14  E-value: 1.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574313  72 KDPSRLLLWAAEKNRLTTVRRLLSEKAThVNTRDEDEYTPLHRAA-YSGHLDIVQELIAQGADVHAVTVDGWTPLHSACK 150
Cdd:PHA02876  306 KGETPLYLMAKNGYDTENIRTLIMLGAD-VNAADRLYITPLHQAStLDRNKDIVITLLELGANVNARDYCDKTPIHYAAV 384

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1034574313 151 WNNTRVASFLLQHDADINAQTKGLLTPLHLA 181
Cdd:PHA02876  385 RNNVVIINTLLDYGADIEALSQKIGTALHFA 415
PHA03095 PHA03095
ankyrin-like protein; Provisional
 101-160 1.94e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 48.10  E-value: 1.94e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034574313 101 VNTRDEDEYTPLHRAAYSGHLDIVQELIAQGADVHAVTVDGWTPLHSACKWNNTR-VASFL 160
Cdd:PHA03095  250 INARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRaVRAAL 310
PHA02946 PHA02946
ankyin-like protein; Provisional
 124-186 2.54e-06

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 47.74  E-value: 2.54e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034574313 124 VQELIAQGADVHAVTVDGWTPLHSACKWNNTRVASFLLQHDADINAQTKGLLTPLHLAAGNRD 186
Cdd:PHA02946   55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDD 117
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 116-195 2.68e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.97  E-value: 2.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574313 116 AYSGHLDIVQELIAQGADVHAVTVDGWTPLHSACKWNNTRVASFLLQHDADINAQTKGLLTPLHLAAGNrDSKDTLELLL 195
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEEN-GFREVVQLLS 168
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 140-169 3.42e-06

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 42.63  E-value: 3.42e-06
                          10        20        30
                  ....*....|....*....|....*....|
gi 1034574313 140 DGWTPLHSACKWNNTRVASFLLQHDADINA 169
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 60-180 3.66e-06

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: 47.31  E-value: 3.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574313  60 EEWYRLQEKKMEKDPsrlLLWAAEKNRLTTVRRLLS-------------EKATHV---NTRDE----------------- 106
Cdd:cd22192     6 DELHLLQQKRISESP---LLLAAKENDVQAIKKLLKcpscdlfqrgalgETALHVaalYDNLEaavvlmeaapelvnepm 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574313 107 --DEY---TPLHRAAYSGHLDIVQELIAQGADV--------------HAVTVDGWTPLHSACKWNNTRVASFLLQHDADI 167
Cdd:cd22192    83 tsDLYqgeTALHIAVVNQNLNLVRELIARGADVvspratgtffrpgpKNLIYYGEHPLSFAACVGNEEIVRLLIEHGADI 162

                         170
                  ....*....|...
gi 1034574313 168 NAQTKGLLTPLHL 180
Cdd:cd22192   163 RAQDSLGNTVLHI 175
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 140-169 4.74e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.19  E-value: 4.74e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 1034574313  140 DGWTPLHSACKWNNTRVASFLLQHDADINA 169
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
127-181 7.28e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 7.28e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034574313 127 LIAQG-ADVHAVTVDGWTPLHSACKWNNTRVASFLLQHDADINAQTKGLLTPLHLA 181
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 107-138 9.15e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 41.51  E-value: 9.15e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1034574313 107 DEYTPLHRAAYS-GHLDIVQELIAQGADVHAVT 138
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
PHA03095 PHA03095
ankyrin-like protein; Provisional
 88-191 1.29e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 45.40  E-value: 1.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574313  88 TTVRRLLSEKATHVNTRDEDEYTPLHRAAYSGH--LDIVQELIAQGADVHAVTVDGWTPLHSACKW--NNTRVASFLLQH 163
Cdd:PHA03095  132 PKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanVELLRLLIDAGADVYAVDDRFRSLLHHHLQSfkPRARIVRELIRA 211

                          90       100
                  ....*....|....*....|....*...
gi 1034574313 164 DADINAQTKGLLTPLHLAAGNRDSKDTL 191
Cdd:PHA03095  212 GCDPAATDMLGNTPLHSMATGSSCKRSL 239
PHA02798 PHA02798
ankyrin-like protein; Provisional
 92-195 1.63e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 45.21  E-value: 1.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574313  92 RLLSEKATHVNTRDEDEYTPL-----HRAAYSGHLDIVQELIAQGADVHAVTVDGWTPLH---SACKWNNTRVASFLLQH 163
Cdd:PHA02798   55 KLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYcllSNGYINNLEILLFMIEN 134

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1034574313 164 DADINAQTKGLLTPL--HLAAGNRDSKDTLELLL 195
Cdd:PHA02798  135 GADTTLLDKDGFTMLqvYLQSNHHIDIEIIKLLL 168
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 107-136 2.19e-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: 40.26  E-value: 2.19e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 1034574313  107 DEYTPLHRAAYSGHLDIVQELIAQGADVHA 136
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 107-136 2.33e-05

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 40.32  E-value: 2.33e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 1034574313 107 DEYTPLHRAAYSGHLDIVQELIAQGADVHA 136
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 77-145 7.00e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 43.70  E-value: 7.00e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574313  77 LLLWAAEKNRLTTVRRLLsEKATHVNTRDEDEYTPLHRAAYSGHLDIVQELIAQGADV-HAVTVDGWTPL 145
Cdd:PLN03192  625 LLCTAAKRNDLTAMKELL-KQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVdKANTDDDFSPT 693
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 115-200 1.32e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 42.29  E-value: 1.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574313 115 AAYSGHLDIVQELIAQGADVHAVTVDGWTPLHSACKWNNTRVASFLLQHDADINAQTKGLLTPLHLAAGNRDSKDTLELL 194
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88


                  ....*.
gi 1034574313 195 LMNRYV 200
Cdd:PHA02875   89 DLGKFA 94
Ank_5 pfam13857
Ankyrin repeats (many copies);
160-216 1.71e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.48  E-value: 1.71e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034574313 160 LLQHD-ADINAQTKGLLTPLHLAAGNRDSkDTLELLLMNRyVKPGLKNNLEETAFDIA 216
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGAL-EIVRVLLAYG-VDLNLKDEEGLTALDLA 56
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 85-167 2.72e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 41.59  E-value: 2.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574313  85 NRLTTVRRLLsEKATHVNTRDEDEYTPLHRAAYSG-HLDIVQELIAQGADVHAVTVDGWTPLHSACKWNNtrVASFLLQH 163
Cdd:PHA02876  420 NPYMSVKTLI-DRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIALEYHG--IVNILLHY 496


                  ....
gi 1034574313 164 DADI 167
Cdd:PHA02876  497 GAEL 500
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 87-230 6.61e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 40.33  E-value: 6.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574313  87 LTTVRRLLSEKATHVNTRDEDEYTPLHRAAYSGHLDIVQELIAQGADVHAVTVDGWTPLHSACKWNNTRVASFLLQHDAD 166
Cdd:PHA02874   14 IEAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVD 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574313 167 -----------------------INAQTKGLLTPLHLAAGNRDskdtleLLLMNRYVKPGLKNNLEETAFDIARRTSIYH 223
Cdd:PHA02874   94 tsilpipciekdmiktildcgidVNIKDAELKTFLHYAIKKGD------LESIKMLFEYGADVNIEDDNGCYPIHIAIKH 167


                  ....*..
gi 1034574313 224 YLFEIVE 230
Cdd:PHA02874  168 NFFDIIK 174
PHA02798 PHA02798
ankyrin-like protein; Provisional
 112-215 8.40e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 40.20  E-value: 8.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574313 112 LHRAAYSghLDIVQELIAQGADVHAVTVDGWTPL---HSACKWNNTR--VASFLLQHDADINAQTKGLLTPLHlaagnrd 186
Cdd:PHA02798   44 LQRDSPS--TDIVKLFINLGANVNGLDNEYSTPLctiLSNIKDYKHMldIVKILIENGADINKKNSDGETPLY------- 114

                          90       100
                  ....*....|....*....|....*....
gi 1034574313 187 skdtleLLLMNRYVkpglkNNLEETAFDI 215
Cdd:PHA02798  115 ------CLLSNGYI-----NNLEILLFMI 132
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 111-161 8.45e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 39.86  E-value: 8.45e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1034574313 111 PLHRAAYSGHLDIVQELIAQGADVHAVTVDGWTPLHSACKWNNTRVASFLL 161
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMI 90
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 79-195 9.14e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 39.97  E-value: 9.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574313  79 LWAAEKNRLTTVRRLLSEKATHVNTRDEDEYTPLHRAAYSGHLDIVQELIAQGADVHAVTVDGWTPLHSACKWNNTRVAS 158
Cdd:PHA02875  106 LHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICK 185

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1034574313 159 FLLQHDADINAQTKGLLTPLHLAAGNRDSKDTLELLL 195
Cdd:PHA02875  186 MLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFI 222
PHA02795 PHA02795
ankyrin-like protein; Provisional
 101-148 1.04e-03

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 39.59  E-value: 1.04e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1034574313 101 VNTRDEDEYTPLHRAAYSGHLDIVQELIAQGADVHAVTVDGWTPLHSA 148
Cdd:PHA02795  214 INQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVA 261
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 100-199 3.91e-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: 38.14  E-value: 3.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574313 100 HVNTRDEDEY----TPLHRAAYSGHLDIVQELIAQGADVHA-------VTVDGWT-------PLHSACKWNNTRVASFLL 161
Cdd:TIGR00870 116 LANDQYTSEFtpgiTALHLAAHRQNYEIVKLLLERGASVPAracgdffVKSQGVDsfyhgesPLNAAACLGSPSIVALLS 195

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1034574313 162 QHDADINAQTKGLLTPLHLAAGNRDSKDTLELLLMNRY 199
Cdd:TIGR00870 196 EDPADILTADSLGNTLLHLLVMENEFKAEYEELSCQMY 233
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 92-160 8.82e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 35.62  E-value: 8.82e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034574313  92 RLLSEKATHVNTRDE-DEYTPLHRAAYSGHLDIVQELIAQ-GADVHAVTVDGWTPLHSACKWNNTRVASFL 160
Cdd:PHA02736   75 KLLMEWGADINGKERvFGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERHDAKMMNIL 145
 
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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