NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|198278513|ref|NP_001119755|]
View 

ankyrin repeat domain-containing protein 49 [Rattus norvegicus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
77-218 9.47e-37

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 130.84  E-value: 9.47e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278513  77 LLLWAAEKNRLATVQRLLsEKAAEVNTRDEDEYTPLHRAAYSGHLDVVRELVAQGADVHAVTIDGWTPLHSACKWNNTRV 156
Cdd:COG0666   90 LLHAAARNGDLEIVKLLL-EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEI 168
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 198278513 157 ASFLLQHDADINAQTKGLLTPLHLAAGNRDsRDTLELLLmNRYIKPELKNNSRETASDIARR 218
Cdd:COG0666  169 VKLLLEAGADVNARDNDGETPLHLAAENGH-LEIVKLLL-EAGADVNAKDNDGKTALDLAAE 228
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
77-218 9.47e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 130.84  E-value: 9.47e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278513  77 LLLWAAEKNRLATVQRLLsEKAAEVNTRDEDEYTPLHRAAYSGHLDVVRELVAQGADVHAVTIDGWTPLHSACKWNNTRV 156
Cdd:COG0666   90 LLHAAARNGDLEIVKLLL-EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEI 168
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 198278513 157 ASFLLQHDADINAQTKGLLTPLHLAAGNRDsRDTLELLLmNRYIKPELKNNSRETASDIARR 218
Cdd:COG0666  169 VKLLLEAGADVNARDNDGETPLHLAAENGH-LEIVKLLL-EAGADVNAKDNDGKTALDLAAE 228
Ank_2 pfam12796
Ankyrin repeats (3 copies);
78-170 9.81e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.94  E-value: 9.81e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278513   78 LLWAAEKNRLATVQRLLSEKAaEVNTRDEDEYTPLHRAAYSGHLDVVRELVAQgADVHAVTiDGWTPLHSACKWNNTRVA 157
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGA-DANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77
                          90
                  ....*....|...
gi 198278513  158 SFLLQHDADINAQ 170
Cdd:pfam12796  78 KLLLEKGADINVK 90
PHA03095 PHA03095
ankyrin-like protein; Provisional
82-215 9.34e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 72.75  E-value: 9.34e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278513  82 AEKNRLATVQRLLSeKAAEVNTRDEDEYTPLH---RAAYSGHLDVVRELVAQGADVHAVTIDGWTPLHSACKWNNT-RVA 157
Cdd:PHA03095  22 ASNVTVEEVRRLLA-AGADVNFRGEYGKTPLHlylHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVI 100
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 198278513 158 SFLLQHDADINAQTKGLLTPLHLAAGNRDSR-DTLELLLmNRYIKPELKNNSRETASDI 215
Cdd:PHA03095 101 KLLIKAGADVNAKDKVGRTPLHVYLSGFNINpKVIRLLL-RKGADVNALDLYGMTPLAV 158
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
140-169 2.29e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.96  E-value: 2.29e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 198278513   140 DGWTPLHSACKWNNTRVASFLLQHDADINA 169
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
60-180 2.13e-05

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: 45.00  E-value: 2.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278513  60 EEWYQLQEKKLEKEPsklLLWAAEKNRLATVQRLLSEKAAEVNTR--------------DEDE----------------- 108
Cdd:cd22192    6 DELHLLQQKRISESP---LLLAAKENDVQAIKKLLKCPSCDLFQRgalgetalhvaalyDNLEaavvlmeaapelvnepm 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278513 109 ----Y---TPLHRAAYSGHLDVVRELVAQGADV--------------HAVTIDGWTPLHSACKWNNTRVASFLLQHDADI 167
Cdd:cd22192   83 tsdlYqgeTALHIAVVNQNLNLVRELIARGADVvspratgtffrpgpKNLIYYGEHPLSFAACVGNEEIVRLLIEHGADI 162
                        170
                 ....*....|...
gi 198278513 168 NAQTKGLLTPLHL 180
Cdd:cd22192  163 RAQDSLGNTVLHI 175
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
52-199 2.63e-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: 41.61  E-value: 2.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278513   52 DDEQEEKNEEWYQLQeKKLEKEPS--KLLLWAAEKNRLATVQRLLS--EKAAE-------VNTRDEDEY----TPLHRAA 116
Cdd:TIGR00870  58 VAAIENENLELTELL-LNLSCRGAvgDTLLHAISLEYVDAVEAILLhlLAAFRksgplelANDQYTSEFtpgiTALHLAA 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278513  117 YSGHLDVVRELVAQGADVHA-------VTIDGWT-------PLHSACKWNNTRVASFLLQHDADINAQTKGLLTPLHLAA 182
Cdd:TIGR00870 137 HRQNYEIVKLLLERGASVPAracgdffVKSQGVDsfyhgesPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLV 216
                         170
                  ....*....|....*..
gi 198278513  183 GNRDSRDTLELLLMNRY 199
Cdd:TIGR00870 217 MENEFKAEYEELSCQMY 233
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
77-218 9.47e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 130.84  E-value: 9.47e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278513  77 LLLWAAEKNRLATVQRLLsEKAAEVNTRDEDEYTPLHRAAYSGHLDVVRELVAQGADVHAVTIDGWTPLHSACKWNNTRV 156
Cdd:COG0666   90 LLHAAARNGDLEIVKLLL-EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEI 168
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 198278513 157 ASFLLQHDADINAQTKGLLTPLHLAAGNRDsRDTLELLLmNRYIKPELKNNSRETASDIARR 218
Cdd:COG0666  169 VKLLLEAGADVNARDNDGETPLHLAAENGH-LEIVKLLL-EAGADVNAKDNDGKTALDLAAE 228
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
77-216 9.62e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 117.75  E-value: 9.62e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278513  77 LLLWAAEKNRLATVQRLLsEKAAEVNTRDEDEYTPLHRAAYSGHLDVVRELVAQGADVHAVTIDGWTPLHSACKWNNTRV 156
Cdd:COG0666  123 PLHLAAYNGNLEIVKLLL-EAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEI 201
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278513 157 ASFLLQHDADINAQTKGLLTPLHLAAGNRDSRdtLELLLMNRYIKPELKNNSRETASDIA 216
Cdd:COG0666  202 VKLLLEAGADVNAKDNDGKTALDLAAENGNLE--IVKLLLEAGADLNAKDKDGLTALLLA 259
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
69-216 1.30e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 109.27  E-value: 1.30e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278513  69 KLEKEPSKLLLWAAEKNRLATVQRLLSEKAAEVNTRDEDEYTPLHRAAYSGHLDVVRELVAQGADVHAVTIDGWTPLHSA 148
Cdd:COG0666   48 ALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLA 127
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 198278513 149 CKWNNTRVASFLLQHDADINAQTKGLLTPLHLAAGNRDsRDTLELLLmNRYIKPELKNNSRETASDIA 216
Cdd:COG0666  128 AYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN-LEIVKLLL-EAGADVNARDNDGETPLHLA 193
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
77-207 7.16e-25

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 99.64  E-value: 7.16e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278513  77 LLLWAAEKNRLATVQRLLsEKAAEVNTRDEDEYTPLHRAAYSGHLDVVRELVAQGADVHAVTIDGWTPLHSACKWNNTRV 156
Cdd:COG0666  156 PLHLAAANGNLEIVKLLL-EAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI 234
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 198278513 157 ASFLLQHDADINAQTKGLLTPLHLAAGNRDSRDTLELLLMNRYIKPELKNN 207
Cdd:COG0666  235 VKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285
Ank_2 pfam12796
Ankyrin repeats (3 copies);
78-170 9.81e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.94  E-value: 9.81e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278513   78 LLWAAEKNRLATVQRLLSEKAaEVNTRDEDEYTPLHRAAYSGHLDVVRELVAQgADVHAVTiDGWTPLHSACKWNNTRVA 157
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGA-DANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77
                          90
                  ....*....|...
gi 198278513  158 SFLLQHDADINAQ 170
Cdd:pfam12796  78 KLLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
112-206 4.20e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.01  E-value: 4.20e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278513  112 LHRAAYSGHLDVVRELVAQGADVHAVTIDGWTPLHSACKWNNTRVASFLLQHdADINAQTKGlLTPLHLAAGNRdSRDTL 191
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG-RTALHYAARSG-HLEIV 77
                          90
                  ....*....|....*
gi 198278513  192 ELLLMNrYIKPELKN 206
Cdd:pfam12796  78 KLLLEK-GADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
56-212 1.88e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 73.83  E-value: 1.88e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278513  56 EEKNEEWYQLQEKKLEKEPSKLLLWAAEKNRLATVQRLLSEKAAEVNTRDEDEYTPLHRAAYSGHLDVVRELVAQGADVH 135
Cdd:COG0666    2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 198278513 136 AVTIDGWTPLHSACKWNNTRVASFLLQHDADINAQTKGLLTPLHLAAGNRDsRDTLELLLmNRYIKPELKNNSRETA 212
Cdd:COG0666   82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGN-LEIVKLLL-EAGADVNAQDNDGNTP 156
Ank_4 pfam13637
Ankyrin repeats (many copies);
108-161 3.60e-15

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 67.30  E-value: 3.60e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 198278513  108 EYTPLHRAAYSGHLDVVRELVAQGADVHAVTIDGWTPLHSACKWNNTRVASFLL 161
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
82-215 9.34e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 72.75  E-value: 9.34e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278513  82 AEKNRLATVQRLLSeKAAEVNTRDEDEYTPLH---RAAYSGHLDVVRELVAQGADVHAVTIDGWTPLHSACKWNNT-RVA 157
Cdd:PHA03095  22 ASNVTVEEVRRLLA-AGADVNFRGEYGKTPLHlylHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVI 100
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 198278513 158 SFLLQHDADINAQTKGLLTPLHLAAGNRDSR-DTLELLLmNRYIKPELKNNSRETASDI 215
Cdd:PHA03095 101 KLLIKAGADVNAKDKVGRTPLHVYLSGFNINpKVIRLLL-RKGADVNALDLYGMTPLAV 158
PHA03100 PHA03100
ankyrin repeat protein; Provisional
84-169 2.06e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 71.62  E-value: 2.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278513  84 KNRlatVQRLLSeKAAEVNTRDEDEYTPLHRAAYSGHLDVVRELVAQGADVHAVTIDGWTPLHSACKWNNTRVASFLLQH 163
Cdd:PHA03100 172 KNR---VNYLLS-YGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNN 247

                 ....*.
gi 198278513 164 DADINA 169
Cdd:PHA03100 248 GPSIKT 253
PHA02874 PHA02874
ankyrin repeat protein; Provisional
71-225 3.52e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 68.07  E-value: 3.52e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278513  71 EKEPSKLLLWAAEKNRLATVQRLLsEKAAEVNTRDEDEYTPLHRAAYSGHLDVVRELVAQGADVHAVTIDGWTPLHSACK 150
Cdd:PHA02874 121 DAELKTFLHYAIKKGDLESIKMLF-EYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAE 199
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 198278513 151 WNNTRVASFLLQHDADINAQTKGLLTPLHLAagnrdsrdtlelLLMNRYIKPELKNNSRETASDIARRTSIYHYL 225
Cdd:PHA02874 200 YGDYACIKLLIDHGNHIMNKCKNGFTPLHNA------------IIHNRSAIELLINNASINDQDIDGSTPLHHAI 262
PHA03095 PHA03095
ankyrin-like protein; Provisional
90-225 6.26e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 67.36  E-value: 6.26e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278513  90 VQRLLSEKAAEVNTRDEDEYTPLHRAAYSGH-LDVVRELVAQGADVHAVTIDGWTPLHSAC--KWNNTRVASFLLQHDAD 166
Cdd:PHA03095  65 IVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGADVNAKDKVGRTPLHVYLsgFNINPKVIRLLLRKGAD 144
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278513 167 INAQTKGLLTPLHLAAGNRD-SRDTLELLlmnryikpeLKNNSRETASDIARRTSIYHYL 225
Cdd:PHA03095 145 VNALDLYGMTPLAVLLKSRNaNVELLRLL---------IDAGADVYAVDDRFRSLLHHHL 195
PHA02878 PHA02878
ankyrin repeat protein; Provisional
88-195 7.66e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 64.13  E-value: 7.66e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278513  88 ATVQRLLSEKAAEVNTRDEDE-YTPLHRAAYSGHLDVVRELVAQGADVHAVTIDGWTPLHSACKWNNTRVASFLLQHDAD 166
Cdd:PHA02878 147 AEITKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS 226
                         90       100
                 ....*....|....*....|....*....
gi 198278513 167 INAQTKGLLTPLHLAAGNRDSRDTLELLL 195
Cdd:PHA02878 227 TDARDKCGNTPLHISVGYCKDYDILKLLL 255
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
78-178 4.41e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 61.51  E-value: 4.41e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278513  78 LLWAAEKNRLATVQRLLsEKAAEVNTRDEDEYTPLHRAAYSGHLDVVRELVAQGADVHAVTIDGWTPLHSACKWNNTRVA 157
Cdd:COG0666  190 LHLAAENGHLEIVKLLL-EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIV 268
                         90       100
                 ....*....|....*....|.
gi 198278513 158 SFLLQHDADINAQTKGLLTPL 178
Cdd:COG0666  269 KLLLLALLLLAAALLDLLTLL 289
PHA02876 PHA02876
ankyrin repeat protein; Provisional
94-197 1.76e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 60.46  E-value: 1.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278513  94 LSEKAAEVNTRDEDEYTPLHRAAYSGHLDVVRELVAQGADVHAVTIDGWTPLHSA-CKWNNTRVASFLLQHDADINAQTK 172
Cdd:PHA02876 361 LLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNK 440
                         90       100
                 ....*....|....*....|....*
gi 198278513 173 GLLTPLHLAAGNRDSRDTLELLLMN 197
Cdd:PHA02876 441 DLSTPLHYACKKNCKLDVIEMLLDN 465
PHA02874 PHA02874
ankyrin repeat protein; Provisional
82-216 2.29e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 59.98  E-value: 2.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278513  82 AEKNRLATVQRLLSEKAAEVNTRDEDEYTPLHRAAYSGHLDVVRELVAQGADVHAVTIDGWTPLHSACKWNntRVASFLL 161
Cdd:PHA02874 164 AIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHN--RSAIELL 241
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 198278513 162 QHDADINAQTKGLLTPLHLAAGNRDSRDTLELLLMNRyIKPELKNNSRETASDIA 216
Cdd:PHA02874 242 INNASINDQDIDGSTPLHHAINPPCDIDIIDILLYHK-ADISIKDNKGENPIDTA 295
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
92-163 2.84e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 59.91  E-value: 2.84e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 198278513  92 RLLSEKAAEVNTRDEDEYTPLHRAAYSGHLDVVRELVAQGADVHAVTIDGWTPLHSACKWNNTRVASFLLQH 163
Cdd:PTZ00322  99 RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PHA02878 PHA02878
ankyrin repeat protein; Provisional
68-195 2.90e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 59.51  E-value: 2.90e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278513  68 KKLEKEPSKLLLWAAEKNRLATVQRLLSEKAAEVNTRDEDEYTPLHRAAYSGHLDVVRELVAQGADVHAVTIDGWTPLH- 146
Cdd:PHA02878 161 NMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHi 240
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 198278513 147 --SACKwnNTRVASFLLQHDADINAQTKGL-LTPLHLAAgnrDSRDTLELLL 195
Cdd:PHA02878 241 svGYCK--DYDILKLLLEHGVDVNAKSYILgLTALHSSI---KSERKLKLLL 287
PHA02878 PHA02878
ankyrin repeat protein; Provisional
79-232 6.11e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 58.74  E-value: 6.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278513  79 LWAAEKNRLATVQRLLSEKAAEVNTRDEDEYTPLHRA-AYSGHLDVVRELVAQGADVHA-VTIDGWTPLHSACKwnNTRV 156
Cdd:PHA02878 205 LHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAkSYILGLTALHSSIK--SERK 282
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278513 157 ASFLLQHDADINAQTKGLLTPLHLAAGNRDSRDTLELLLMN----RYIKPELKNnsreTASDIARRTSIYHY--LFEIAE 230
Cdd:PHA02878 283 LKLLLEYGADINSLNSYKLTPLSSAVKQYLCINIGRILISNicllKRIKPDIKN----SEGFIDNMDCITSNkrLNQIKD 358

                 ..
gi 198278513 231 GC 232
Cdd:PHA02878 359 KC 360
Ank_4 pfam13637
Ankyrin repeats (many copies);
77-128 6.35e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.43  E-value: 6.35e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 198278513   77 LLLWAAEKNRLATVQRLLsEKAAEVNTRDEDEYTPLHRAAYSGHLDVVRELV 128
Cdd:pfam13637   4 ALHAAAASGHLELLRLLL-EKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
77-198 1.89e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 56.98  E-value: 1.89e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278513  77 LLLWAAEKNRLATVQRLLSEKAAEVNTRDEDEYTPLHRAAYSGH--LDVVRELVAQGADVHA-----------VTID--- 140
Cdd:PHA03100 110 LLYAISKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAknrvnyllsygVPINikd 189
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278513 141 --GWTPLHSACKWNNTRVASFLLQHDADINAQTKGLLTPLHLAAGNRDSrDTLELLLMNR 198
Cdd:PHA03100 190 vyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNK-EIFKLLLNNG 248
Ank_5 pfam13857
Ankyrin repeats (many copies);
93-148 3.00e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 51.58  E-value: 3.00e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 198278513   93 LLSEKAAEVNTRDEDEYTPLHRAAYSGHLDVVRELVAQGADVHAVTIDGWTPLHSA 148
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
141-195 1.09e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.97  E-value: 1.09e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 198278513  141 GWTPLHSACKWNNTRVASFLLQHDADINAQTKGLLTPLHLAAGNRDSrDTLELLL 195
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNV-EVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
88-188 1.29e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 54.65  E-value: 1.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278513  88 ATVQRLLSEKAAEVNTRDEDEYTPLHRAAY--SGHLDVVRELVAQGADVHAVTIDGWTPLHSACKWNNTRVASFLLQHDA 165
Cdd:PHA03095 202 ARIVRELIRAGCDPAATDMLGNTPLHSMATgsSCKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGA 281
                         90       100
                 ....*....|....*....|...
gi 198278513 166 DINAQTKGLLTPLHLAAGNRDSR 188
Cdd:PHA03095 282 DINAVSSDGNTPLSLMVRNNNGR 304
PHA02876 PHA02876
ankyrin repeat protein; Provisional
77-224 4.32e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 53.14  E-value: 4.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278513  77 LLLWAAEKNRLATVQRLLSEKAAEVNTRDEDEYTPLHRAAYSGHLD-VVRELVAQGADVHAVTIDGWTPLHSACKWN-NT 154
Cdd:PHA02876 242 LSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGyDT 321
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278513 155 RVASFLLQHDADINAQTKGLLTPLHLAAGNRDSRDTLELLLmnryikpELKNNSreTASDIARRTSIyHY 224
Cdd:PHA02876 322 ENIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIVITLL-------ELGANV--NARDYCDKTPI-HY 381
PHA03100 PHA03100
ankyrin repeat protein; Provisional
83-212 1.03e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 51.97  E-value: 1.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278513  83 EKNRLATVQRL--LSEKAAEVNTRDEDEYTPLHRAAYSGHLDVVRELVAQGADVHAVTIDGWTPLHSACKW-----NNTR 155
Cdd:PHA03100   8 TKSRIIKVKNIkyIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIkynltDVKE 87
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 198278513 156 VASFLLQHDADINAQTKGLLTPLHLAAGNR-DSRDTLELLLMNRyIKPELKNNSRETA 212
Cdd:PHA03100  88 IVKLLLEYGANVNAPDNNGITPLLYAISKKsNSYSIVEYLLDNG-ANVNIKNSDGENL 144
PHA02876 PHA02876
ankyrin repeat protein; Provisional
90-193 1.52e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 51.60  E-value: 1.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278513  90 VQRLLSEKAAEVNTRDEDEYTPLHRAAYSGHLDVVRELVAQGADVHAVTIDGWTPLHSACKWNNTRVASFLLQHDADINA 169
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINK 239
                         90       100
                 ....*....|....*....|....
gi 198278513 170 QTKGLLTplhlAAGNRDSRDTLEL 193
Cdd:PHA02876 240 NDLSLLK----AIRNEDLETSLLL 259
PHA03095 PHA03095
ankyrin-like protein; Provisional
96-160 1.56e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 51.18  E-value: 1.56e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 198278513  96 EKAAEVNTRDEDEYTPLHRAAYSGHLDVVRELVAQGADVHAVTIDGWTPLHSACKWNNTR-VASFL 160
Cdd:PHA03095 245 IAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRaVRAAL 310
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
116-195 1.59e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.44  E-value: 1.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278513 116 AYSGHLDVVRELVAQGADVHAVTIDGWTPLHSACKWNNTRVASFLLQHDADINAQTKGLLTPLHLAAGNrDSRDTLELLL 195
Cdd:PTZ00322  90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEEN-GFREVVQLLS 168
PHA02875 PHA02875
ankyrin repeat protein; Provisional
82-198 5.22e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 49.60  E-value: 5.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278513  82 AEKNRLATVQRLLSEKAAEVNTRDEDEYTPLHRAAYSGHLDVVRELVAQGADVHAVTI-DGWTPLHSACKWNNTRVASFL 160
Cdd:PHA02875  42 AMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYkDGMTPLHLATILKKLDIMKLL 121
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 198278513 161 LQHDADINAQTKGLLTPLHLAAGNRDSRDTlELLLMNR 198
Cdd:PHA02875 122 IARGADPDIPNTDKFSPLHLAVMMGDIKGI-ELLIDHK 158
PHA02876 PHA02876
ankyrin repeat protein; Provisional
92-181 5.27e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 50.06  E-value: 5.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278513  92 RLLSEKAAEVNTRDEDEYTPLHRAA-YSGHLDVVRELVAQGADVHAVTIDGWTPLHSACKWNNTRVASFLLQHDADINAQ 170
Cdd:PHA02876 325 RTLIMLGADVNAADRLYITPLHQAStLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEAL 404
                         90
                 ....*....|.
gi 198278513 171 TKGLLTPLHLA 181
Cdd:PHA02876 405 SQKIGTALHFA 415
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
140-172 6.72e-07

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: 44.59  E-value: 6.72e-07
                          10        20        30
                  ....*....|....*....|....*....|....
gi 198278513  140 DGWTPLHSAC-KWNNTRVASFLLQHDADINAQTK 172
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA02875 PHA02875
ankyrin repeat protein; Provisional
81-186 6.88e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 49.22  E-value: 6.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278513  81 AAEKNRLATVQRLLSEKAAEVNTRDEDEYTPLHRAAYSGHLDVVRELVAQGADVHAVTIDGWTPLHSACKWNNTRVASFL 160
Cdd:PHA02875  75 AVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELL 154
                         90       100
                 ....*....|....*....|....*.
gi 198278513 161 LQHDADINAQTKGLLTPLHLAAGNRD 186
Cdd:PHA02875 155 IDHKACLDIEDCCGCTPLIIAMAKGD 180
PHA03100 PHA03100
ankyrin repeat protein; Provisional
78-175 1.99e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 48.12  E-value: 1.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278513  78 LLWAAEKNRLATVQRLLsEKAAEVNTRDEDEYTPLHRAAYSGHLDVVRELVAQGADVhavtidgwtplhsackwnNTRVA 157
Cdd:PHA03100 196 LHYAVYNNNPEFVKYLL-DLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSI------------------KTIIE 256
                         90
                 ....*....|....*...
gi 198278513 158 SFLLQHDADINAQTKGLL 175
Cdd:PHA03100 257 TLLYFKDKDLNTITKIKM 274
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
140-169 2.10e-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: 43.01  E-value: 2.10e-06
                          10        20        30
                  ....*....|....*....|....*....|
gi 198278513  140 DGWTPLHSACKWNNTRVASFLLQHDADINA 169
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
140-169 2.29e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.96  E-value: 2.29e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 198278513   140 DGWTPLHSACKWNNTRVASFLLQHDADINA 169
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02798 PHA02798
ankyrin-like protein; Provisional
92-195 4.03e-06

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 47.14  E-value: 4.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278513  92 RLLSEKAAEVNTRDEDEYTPL-----HRAAYSGHLDVVRELVAQGADVHAVTIDGWTPLH---SACKWNNTRVASFLLQH 163
Cdd:PHA02798  55 KLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYcllSNGYINNLEILLFMIEN 134
                         90       100       110
                 ....*....|....*....|....*....|....
gi 198278513 164 DADINAQTKGLLTPL--HLAAGNRDSRDTLELLL 195
Cdd:PHA02798 135 GADTTLLDKDGFTMLqvYLQSNHHIDIEIIKLLL 168
PHA02946 PHA02946
ankyin-like protein; Provisional
124-186 4.60e-06

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 46.97  E-value: 4.60e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 198278513 124 VRELVAQGADVHAVTIDGWTPLHSACKWNNTRVASFLLQHDADINAQTKGLLTPLHLAAGNRD 186
Cdd:PHA02946  55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDD 117
PHA02876 PHA02876
ankyrin repeat protein; Provisional
121-198 5.74e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.98  E-value: 5.74e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 198278513 121 LDVVRELVAQGADVHAVTIDGWTPLHSACKWNNTRVASFLLQHDADINAQTKGLLTPLHLAAgNRDSRDTLELLLMNR 198
Cdd:PHA02876 158 LLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAV-DSKNIDTIKAIIDNR 234
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
107-138 8.71e-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: 8.71e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 198278513  107 DEYTPLHRAAYS-GHLDVVRELVAQGADVHAVT 138
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
Ank_5 pfam13857
Ankyrin repeats (many copies);
127-181 8.80e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 8.80e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 198278513  127 LVAQG-ADVHAVTIDGWTPLHSACKWNNTRVASFLLQHDADINAQTKGLLTPLHLA 181
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
107-136 1.40e-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: 1.40e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 198278513   107 DEYTPLHRAAYSGHLDVVRELVAQGADVHA 136
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
60-180 2.13e-05

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: 45.00  E-value: 2.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278513  60 EEWYQLQEKKLEKEPsklLLWAAEKNRLATVQRLLSEKAAEVNTR--------------DEDE----------------- 108
Cdd:cd22192    6 DELHLLQQKRISESP---LLLAAKENDVQAIKKLLKCPSCDLFQRgalgetalhvaalyDNLEaavvlmeaapelvnepm 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278513 109 ----Y---TPLHRAAYSGHLDVVRELVAQGADV--------------HAVTIDGWTPLHSACKWNNTRVASFLLQHDADI 167
Cdd:cd22192   83 tsdlYqgeTALHIAVVNQNLNLVRELIARGADVvspratgtffrpgpKNLIYYGEHPLSFAACVGNEEIVRLLIEHGADI 162
                        170
                 ....*....|...
gi 198278513 168 NAQTKGLLTPLHL 180
Cdd:cd22192  163 RAQDSLGNTVLHI 175
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
107-136 3.19e-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: 3.19e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 198278513  107 DEYTPLHRAAYSGHLDVVRELVAQGADVHA 136
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02875 PHA02875
ankyrin repeat protein; Provisional
115-200 7.26e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 43.06  E-value: 7.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278513 115 AAYSGHLDVVRELVAQGADVHAVTIDGWTPLHSACKWNNTRVASFLLQHDADINAQTKGLLTPLHLAAGNRDSRDTLELL 194
Cdd:PHA02875   9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88

                 ....*.
gi 198278513 195 LMNRYI 200
Cdd:PHA02875  89 DLGKFA 94
PHA02876 PHA02876
ankyrin repeat protein; Provisional
92-167 1.14e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 42.74  E-value: 1.14e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 198278513  92 RLLSEKAAEVNTRDEDEYTPLHRAAYSG-HLDVVRELVAQGADVHAVTIDGWTPLHSACKWNNtrVASFLLQHDADI 167
Cdd:PHA02876 426 KTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIALEYHG--IVNILLHYGAEL 500
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
77-145 1.31e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 42.55  E-value: 1.31e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278513  77 LLLWAAEKNRLATVQRLLsEKAAEVNTRDEDEYTPLHRAAYSGHLDVVRELVAQGADV-HAVTIDGWTPL 145
Cdd:PLN03192 625 LLCTAAKRNDLTAMKELL-KQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVdKANTDDDFSPT 693
PHA02875 PHA02875
ankyrin repeat protein; Provisional
79-168 2.20e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 41.90  E-value: 2.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278513  79 LWAAEKNRLATVQRLLSEKAAEVNTRDEDEYTPLHRAAYSGHLDVVRELVAQGADVHAVTIDGWTPLHSACKWNNTRVAS 158
Cdd:PHA02875 106 LHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICK 185
                         90
                 ....*....|
gi 198278513 159 FLLQHDADIN 168
Cdd:PHA02875 186 MLLDSGANID 195
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
52-199 2.63e-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: 41.61  E-value: 2.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278513   52 DDEQEEKNEEWYQLQeKKLEKEPS--KLLLWAAEKNRLATVQRLLS--EKAAE-------VNTRDEDEY----TPLHRAA 116
Cdd:TIGR00870  58 VAAIENENLELTELL-LNLSCRGAvgDTLLHAISLEYVDAVEAILLhlLAAFRksgplelANDQYTSEFtpgiTALHLAA 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278513  117 YSGHLDVVRELVAQGADVHA-------VTIDGWT-------PLHSACKWNNTRVASFLLQHDADINAQTKGLLTPLHLAA 182
Cdd:TIGR00870 137 HRQNYEIVKLLLERGASVPAracgdffVKSQGVDsfyhgesPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLV 216
                         170
                  ....*....|....*..
gi 198278513  183 GNRDSRDTLELLLMNRY 199
Cdd:TIGR00870 217 MENEFKAEYEELSCQMY 233
PHA02736 PHA02736
Viral ankyrin protein; Provisional
92-160 4.11e-04

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 39.47  E-value: 4.11e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 198278513  92 RLLSEKAAEVNTRDE-DEYTPLHRAAYSGHLDVVRELVAQ-GADVHAVTIDGWTPLHSACKWNNTRVASFL 160
Cdd:PHA02736  75 KLLMEWGADINGKERvFGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERHDAKMMNIL 145
PHA02878 PHA02878
ankyrin repeat protein; Provisional
111-227 1.13e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 39.48  E-value: 1.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278513 111 PLHRAAYSGHLDVVRELVAQGADVHAVTIDGWTPLHSACKWNN------------------------------------- 153
Cdd:PHA02878  40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNklgmkemirsinkcsvfytlvaikdafnnrnveifki 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278513 154 ---------------------------TRVASFLLQHDADINAQTKGLL-TPLHLAAGNRDSRDTLELLLMNRYIK-PEL 204
Cdd:PHA02878 120 iltnrykniqtidlvyidkkskddiieAEITKLLLSYGADINMKDRHKGnTALHYATENKDQRLTELLLSYGANVNiPDK 199
                        170       180
                 ....*....|....*....|...
gi 198278513 205 KNNSRETASDIARRTSIYHYLFE 227
Cdd:PHA02878 200 TNNSPLHHAVKHYNKPIVHILLE 222
PHA02795 PHA02795
ankyrin-like protein; Provisional
100-148 1.28e-03

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 39.59  E-value: 1.28e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 198278513 100 EVNTRDEDEYTPLHRAAYSGHLDVVRELVAQGADVHAVTIDGWTPLHSA 148
Cdd:PHA02795 213 DINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVA 261
Ank_5 pfam13857
Ankyrin repeats (many copies);
160-216 2.12e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.40  E-value: 2.12e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 198278513  160 LLQHD-ADINAQTKGLLTPLHLAAGNRDSRDtLELLLMNRYiKPELKNNSRETASDIA 216
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEI-VRVLLAYGV-DLNLKDEEGLTALDLA 56
PHA02798 PHA02798
ankyrin-like protein; Provisional
90-215 4.75e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 37.89  E-value: 4.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278513  90 VQRLLSEKAAEVNTRDEDEYTPLH---RAAYSGHLDVVRELVAQGADVHAVTIDGWTPLHSACKWNNT---RVASFLLQH 163
Cdd:PHA02798  91 IVKILIENGADINKKNSDGETPLYcllSNGYINNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEK 170
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 198278513 164 DADINAQT-KGLLTPLHLAAG---NRDSRDTLELLLMNRYIKPELKNNSRETASDI 215
Cdd:PHA02798 171 GVDINTHNnKEKYDTLHCYFKyniDRIDADILKLFVDNGFIINKENKSHKKKFMEY 226
PHA02874 PHA02874
ankyrin repeat protein; Provisional
87-166 4.91e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 37.64  E-value: 4.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278513  87 LATVQRLLSEKAAEVNTRDEDEYTPLHRAAYSGHLDVVRELVAQGADVHAVTIDGWTPLHSACKWNNTRVASFLLQHDAD 166
Cdd:PHA02874  14 IEAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVD 93
PHA02874 PHA02874
ankyrin repeat protein; Provisional
117-197 5.28e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 37.64  E-value: 5.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278513 117 YSGHLDVVRELVAQGADVHAVTID-GWTPLHSACKWNNTRVASFLLQHDADINAQTKGLLTPLhLAAGNRDSRDTLELLL 195
Cdd:PHA02874  10 YSGDIEAIEKIIKNKGNCINISVDeTTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPL-LTAIKIGAHDIIKLLI 88

                 ..
gi 198278513 196 MN 197
Cdd:PHA02874  89 DN 90
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH