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Conserved domains on  [gi|1134612274|ref|NP_001335189|]
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ankyrin repeat domain-containing protein 49 [Mus musculus]

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];
76-217 2.43e-37

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 132.39  E-value: 2.43e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134612274  76 LLLWAAEKNRLATVQRLLsEKAAEVNTRDEDEYTPLHRAAYSGHIDVVRELVAKGADVHAVTVDGWTPLHSACKWNNTKV 155
Cdd:COG0666    90 LLHAAARNGDLEIVKLLL-EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEI 168

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1134612274 156 ASFLLQHDADINAQTKGLLTPLHLAAGNRDsRDTLELLLmNRYIKPELKNNSQETASDIARR 217
Cdd:COG0666   169 VKLLLEAGADVNARDNDGETPLHLAAENGH-LEIVKLLL-EAGADVNAKDNDGKTALDLAAE 228
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
76-217 2.43e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 132.39  E-value: 2.43e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134612274  76 LLLWAAEKNRLATVQRLLsEKAAEVNTRDEDEYTPLHRAAYSGHIDVVRELVAKGADVHAVTVDGWTPLHSACKWNNTKV 155
Cdd:COG0666    90 LLHAAARNGDLEIVKLLL-EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEI 168

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1134612274 156 ASFLLQHDADINAQTKGLLTPLHLAAGNRDsRDTLELLLmNRYIKPELKNNSQETASDIARR 217
Cdd:COG0666   169 VKLLLEAGADVNARDNDGETPLHLAAENGH-LEIVKLLL-EAGADVNAKDNDGKTALDLAAE 228
Ank_2 pfam12796
Ankyrin repeats (3 copies);
77-169 1.99e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.48  E-value: 1.99e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134612274  77 LLWAAEKNRLATVQRLLSEKAaEVNTRDEDEYTPLHRAAYSGHIDVVRELVAKgADVhAVTVDGWTPLHSACKWNNTKVA 156
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGA-DANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADV-NLKDNGRTALHYAARSGHLEIV 77

                          90
                  ....*....|...
gi 1134612274 157 SFLLQHDADINAQ 169
Cdd:pfam12796  78 KLLLEKGADINVK 90
PHA03095 PHA03095
ankyrin-like protein; Provisional
 89-224 1.45e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 72.36  E-value: 1.45e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134612274  89 VQRLLSEKAAEVNTRDEDEYTPLHRAAYSGH-IDVVRELVAKGADVHAVTVDGWTPLHSAC--KWNNTKVASFLLQHDAD 165
Cdd:PHA03095   65 IVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGADVNAKDKVGRTPLHVYLsgFNINPKVIRLLLRKGAD 144

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134612274 166 INAQTKGLLTPLHLAAGNRD-SRDTLELLlmnryikpeLKNNSQETASDIARRTSIYHYL 224
Cdd:PHA03095  145 VNALDLYGMTPLAVLLKSRNaNVELLRLL---------IDAGADVYAVDDRFRSLLHHHL 195
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 139-168 1.48e-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: 43.73  E-value: 1.48e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 1134612274  139 DGWTPLHSACKWNNTKVASFLLQHDADINA 168
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 62-179 5.98e-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: 46.54  E-value: 5.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134612274  62 YQLQEKKMEKDPsklLLWAAEKNRLATVQRLLSEKAAEVNTR--------------DEDE-------------------- 107
Cdd:cd22192     9 HLLQQKRISESP---LLLAAKENDVQAIKKLLKCPSCDLFQRgalgetalhvaalyDNLEaavvlmeaapelvnepmtsd 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134612274 108 -Y---TPLHRAAYSGHIDVVRELVAKGADV--------------HAVTVDGWTPLHSACKWNNTKVASFLLQHDADINAQ 169
Cdd:cd22192    86 lYqgeTALHIAVVNQNLNLVRELIARGADVvspratgtffrpgpKNLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQ 165

                         170
                  ....*....|
gi 1134612274 170 TKGLLTPLHL 179
Cdd:cd22192   166 DSLGNTVLHI 175
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 64-198 4.01e-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: 41.22  E-value: 4.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134612274  64 LQEKKMEKDPSKLLLWAAEKNRLATVQRLLS--EKAAE-------VNTRDEDEY----TPLHRAAYSGHIDVVRELVAKG 130
Cdd:TIGR00870  72 LLNLSCRGAVGDTLLHAISLEYVDAVEAILLhlLAAFRksgplelANDQYTSEFtpgiTALHLAAHRQNYEIVKLLLERG 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134612274 131 ADVHA-------VTVDGWT-------PLHSACKWNNTKVASFLLQHDADINAQTKGLLTPLHLAAGNRDSRDTLELLLMN 196
Cdd:TIGR00870 152 ASVPAracgdffVKSQGVDsfyhgesPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVMENEFKAEYEELSCQ 231


                  ..
gi 1134612274 197 RY 198
Cdd:TIGR00870 232 MY 233
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
76-217 2.43e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 132.39  E-value: 2.43e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134612274  76 LLLWAAEKNRLATVQRLLsEKAAEVNTRDEDEYTPLHRAAYSGHIDVVRELVAKGADVHAVTVDGWTPLHSACKWNNTKV 155
Cdd:COG0666    90 LLHAAARNGDLEIVKLLL-EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEI 168

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1134612274 156 ASFLLQHDADINAQTKGLLTPLHLAAGNRDsRDTLELLLmNRYIKPELKNNSQETASDIARR 217
Cdd:COG0666   169 VKLLLEAGADVNARDNDGETPLHLAAENGH-LEIVKLLL-EAGADVNAKDNDGKTALDLAAE 228
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
76-217 5.07e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 118.52  E-value: 5.07e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134612274  76 LLLWAAEKNRLATVQRLLsEKAAEVNTRDEDEYTPLHRAAYSGHIDVVRELVAKGADVHAVTVDGWTPLHSACKWNNTKV 155
Cdd:COG0666   123 PLHLAAYNGNLEIVKLLL-EAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEI 201

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1134612274 156 ASFLLQHDADINAQTKGLLTPLHLAAGNRDSRdtLELLLMNRYIKPELKNNSQETASDIARR 217
Cdd:COG0666   202 VKLLLEAGADVNAKDNDGKTALDLAAENGNLE--IVKLLLEAGADLNAKDKDGLTALLLAAA 261
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
71-215 3.95e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 110.81  E-value: 3.95e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134612274  71 KDPSKLLLWAAEKNRLATVQRLLSEKAAEVNTRDEDEYTPLHRAAYSGHIDVVRELVAKGADVHAVTVDGWTPLHSACKW 150
Cdd:COG0666    51 DALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYN 130

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1134612274 151 NNTKVASFLLQHDADINAQTKGLLTPLHLAAGNRDsRDTLELLLmNRYIKPELKNNSQETASDIA 215
Cdd:COG0666   131 GNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN-LEIVKLLL-EAGADVNARDNDGETPLHLA 193
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
76-206 4.61e-25

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 100.03  E-value: 4.61e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134612274  76 LLLWAAEKNRLATVQRLLsEKAAEVNTRDEDEYTPLHRAAYSGHIDVVRELVAKGADVHAVTVDGWTPLHSACKWNNTKV 155
Cdd:COG0666   156 PLHLAAANGNLEIVKLLL-EAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI 234

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1134612274 156 ASFLLQHDADINAQTKGLLTPLHLAAGNRDSRDTLELLLMNRYIKPELKNN 206
Cdd:COG0666   235 VKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285
Ank_2 pfam12796
Ankyrin repeats (3 copies);
77-169 1.99e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.48  E-value: 1.99e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134612274  77 LLWAAEKNRLATVQRLLSEKAaEVNTRDEDEYTPLHRAAYSGHIDVVRELVAKgADVhAVTVDGWTPLHSACKWNNTKVA 156
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGA-DANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADV-NLKDNGRTALHYAARSGHLEIV 77

                          90
                  ....*....|...
gi 1134612274 157 SFLLQHDADINAQ 169
Cdd:pfam12796  78 KLLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
111-205 3.36e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.40  E-value: 3.36e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134612274 111 LHRAAYSGHIDVVRELVAKGADVHAVTVDGWTPLHSACKWNNTKVASFLLQHdADINAQTKGlLTPLHLAAGNRdSRDTL 190
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG-RTALHYAARSG-HLEIV 77

                          90
                  ....*....|....*
gi 1134612274 191 ELLLMNrYIKPELKN 205
Cdd:pfam12796  78 KLLLEK-GADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
76-211 1.19e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 74.22  E-value: 1.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134612274  76 LLLWAAEKNRLATVQRLLSEKAAEVNTRDEDEYTPLHRAAYSGHIDVVRELVAKGADVHAVTVDGWTPLHSACKWNNTKV 155
Cdd:COG0666    23 LLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEI 102

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1134612274 156 ASFLLQHDADINAQTKGLLTPLHLAAGNRDsRDTLELLLmNRYIKPELKNNSQETA 211
Cdd:COG0666   103 VKLLLEAGADVNARDKDGETPLHLAAYNGN-LEIVKLLL-EAGADVNAQDNDGNTP 156
Ank_4 pfam13637
Ankyrin repeats (many copies);
107-160 6.99e-15

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 66.53  E-value: 6.99e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1134612274 107 EYTPLHRAAYSGHIDVVRELVAKGADVHAVTVDGWTPLHSACKWNNTKVASFLL 160
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 89-224 1.45e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 72.36  E-value: 1.45e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134612274  89 VQRLLSEKAAEVNTRDEDEYTPLHRAAYSGH-IDVVRELVAKGADVHAVTVDGWTPLHSAC--KWNNTKVASFLLQHDAD 165
Cdd:PHA03095   65 IVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGADVNAKDKVGRTPLHVYLsgFNINPKVIRLLLRKGAD 144

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134612274 166 INAQTKGLLTPLHLAAGNRD-SRDTLELLlmnryikpeLKNNSQETASDIARRTSIYHYL 224
Cdd:PHA03095  145 VNALDLYGMTPLAVLLKSRNaNVELLRLL---------IDAGADVYAVDDRFRSLLHHHL 195
PHA03095 PHA03095
ankyrin-like protein; Provisional
 81-214 2.25e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 71.59  E-value: 2.25e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134612274  81 AEKNRLATVQRLLSeKAAEVNTRDEDEYTPLH---RAAYSGHIDVVRELVAKGADVHAVTVDGWTPLHSACKWNNT-KVA 156
Cdd:PHA03095   22 ASNVTVEEVRRLLA-AGADVNFRGEYGKTPLHlylHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVI 100

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1134612274 157 SFLLQHDADINAQTKGLLTPLHLAAGNRDSR-DTLELLLmNRYIKPELKNNSQETASDI 214
Cdd:PHA03095  101 KLLIKAGADVNAKDKVGRTPLHVYLSGFNINpKVIRLLL-RKGADVNALDLYGMTPLAV 158
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 83-168 3.97e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 70.85  E-value: 3.97e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134612274  83 KNRlatVQRLLSeKAAEVNTRDEDEYTPLHRAAYSGHIDVVRELVAKGADVHAVTVDGWTPLHSACKWNNTKVASFLLQH 162
Cdd:PHA03100  172 KNR---VNYLLS-YGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNN 247


                  ....*.
gi 1134612274 163 DADINA 168
Cdd:PHA03100  248 GPSIKT 253
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 76-224 1.00e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 69.61  E-value: 1.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134612274  76 LLLWAAEKNRLATVQRLLsEKAAEVNTRDEDEYTPLHRAAYSGHIDVVRELVAKGADVHAVTVDGWTPLHSACKWNNTKV 155
Cdd:PHA02874  127 FLHYAIKKGDLESIKMLF-EYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYAC 205

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1134612274 156 ASFLLQHDADINAQTKGLLTPLHLAagnrdsrdtlelLLMNRYIKPELKNNSQETASDIARRTSIYHYL 224
Cdd:PHA02874  206 IKLLIDHGNHIMNKCKNGFTPLHNA------------IIHNRSAIELLINNASINDQDIDGSTPLHHAI 262
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 87-194 3.00e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 65.29  E-value: 3.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134612274  87 ATVQRLLSEKAAEVNTRDEDE-YTPLHRAAYSGHIDVVRELVAKGADVHAVTVDGWTPLHSACKWNNTKVASFLLQHDAD 165
Cdd:PHA02878  147 AEITKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS 226

                          90       100
                  ....*....|....*....|....*....
gi 1134612274 166 INAQTKGLLTPLHLAAGNRDSRDTLELLL 194
Cdd:PHA02878  227 TDARDKCGNTPLHISVGYCKDYDILKLLL 255
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
77-177 3.58e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 61.51  E-value: 3.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134612274  77 LLWAAEKNRLATVQRLLsEKAAEVNTRDEDEYTPLHRAAYSGHIDVVRELVAKGADVHAVTVDGWTPLHSACKWNNTKVA 156
Cdd:COG0666   190 LHLAAENGHLEIVKLLL-EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIV 268

                          90       100
                  ....*....|....*....|.
gi 1134612274 157 SFLLQHDADINAQTKGLLTPL 177
Cdd:COG0666   269 KLLLLALLLLAAALLDLLTLL 289
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 93-196 8.67e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 61.23  E-value: 8.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134612274  93 LSEKAAEVNTRDEDEYTPLHRAAYSGHIDVVRELVAKGADVHAVTVDGWTPLHSA-CKWNNTKVASFLLQHDADINAQTK 171
Cdd:PHA02876  361 LLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNK 440

                          90       100
                  ....*....|....*....|....*
gi 1134612274 172 GLLTPLHLAAGNRDSRDTLELLLMN 196
Cdd:PHA02876  441 DLSTPLHYACKKNCKLDVIEMLLDN 465
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 67-194 1.12e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 60.66  E-value: 1.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134612274  67 KKMEKDPSKLLLWAAEKNRLATVQRLLSEKAAEVNTRDEDEYTPLHRAAYSGHIDVVRELVAKGADVHAVTVDGWTPLH- 145
Cdd:PHA02878  161 NMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHi 240

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1134612274 146 SACKWNNTKVASFLLQHDADINAQTKGL-LTPLHLAAgnrDSRDTLELLL 194
Cdd:PHA02878  241 SVGYCKDYDILKLLLEHGVDVNAKSYILgLTALHSSI---KSERKLKLLL 287
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 91-162 1.61e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 60.30  E-value: 1.61e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1134612274  91 RLLSEKAAEVNTRDEDEYTPLHRAAYSGHIDVVRELVAKGADVHAVTVDGWTPLHSACKWNNTKVASFLLQH 162
Cdd:PTZ00322   99 RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 81-215 2.72e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 59.59  E-value: 2.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134612274  81 AEKNRLATVQRLLSEKAAEVNTRDEDEYTPLHRAAYSGHIDVVRELVAKGADVHAVTVDGWTPLHSACKWNNTKVAsfLL 160
Cdd:PHA02874  164 AIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIE--LL 241

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1134612274 161 QHDADINAQTKGLLTPLHLAAGNRDSRDTLELLLMNRyIKPELKNNSQETASDIA 215
Cdd:PHA02874  242 INNASINDQDIDGSTPLHHAINPPCDIDIIDILLYHK-ADISIKDNKGENPIDTA 295
Ank_4 pfam13637
Ankyrin repeats (many copies);
76-127 8.44e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.05  E-value: 8.44e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1134612274  76 LLLWAAEKNRLATVQRLLsEKAAEVNTRDEDEYTPLHRAAYSGHIDVVRELV 127
Cdd:pfam13637   4 ALHAAAASGHLELLRLLL-EKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 76-197 1.10e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 57.75  E-value: 1.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134612274  76 LLLWAAEKNRLATVQRLLSEKAAEVNTRDEDEYTPLHRAAYSGHID--VVRELVAKGADVHAVT-VD------------- 139
Cdd:PHA03100  110 LLYAISKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDINAKNrVNyllsygvpinikd 189

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134612274 140 --GWTPLHSACKWNNTKVASFLLQHDADINAQTKGLLTPLHLAAGNRDSrDTLELLLMNR 197
Cdd:PHA03100  190 vyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNK-EIFKLLLNNG 248
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 78-205 2.40e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 56.81  E-value: 2.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134612274  78 LWAAEKNRLATVQRLLSEKAAEVNTRDEDEYTPLHRA-AYSGHIDVVRELVAKGADVHA-VTVDGWTPLHSACKwnNTKV 155
Cdd:PHA02878  205 LHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAkSYILGLTALHSSIK--SERK 282

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1134612274 156 ASFLLQHDADINAQTKGLLTPLHLAAGNRDSRDTLELLLMN----RYIKPELKN 205
Cdd:PHA02878  283 LKLLLEYGADINSLNSYKLTPLSSAVKQYLCINIGRILISNicllKRIKPDIKN 336
Ank_5 pfam13857
Ankyrin repeats (many copies);
92-147 2.55e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 51.96  E-value: 2.55e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1134612274  92 LLSEKAAEVNTRDEDEYTPLHRAAYSGHIDVVRELVAKGADVHAVTVDGWTPLHSA 147
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03095 PHA03095
ankyrin-like protein; Provisional
 87-187 5.16e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 55.80  E-value: 5.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134612274  87 ATVQRLLSEKAAEVNTRDEDEYTPLHRAAY--SGHIDVVRELVAKGADVHAVTVDGWTPLHSACKWNNTKVASFLLQHDA 164
Cdd:PHA03095  202 ARIVRELIRAGCDPAATDMLGNTPLHSMATgsSCKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGA 281

                          90       100
                  ....*....|....*....|...
gi 1134612274 165 DINAQTKGLLTPLHLAAGNRDSR 187
Cdd:PHA03095  282 DINAVSSDGNTPLSLMVRNNNGR 304
PHA03095 PHA03095
ankyrin-like protein; Provisional
 87-190 8.84e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 55.03  E-value: 8.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134612274  87 ATVQRLLSEKAAEVNTRDEDEYTPLHRAAYSGHIDV--VRELVAKGADVHAVTVDGWTPLHS---ACKWNNTKVASfLLQ 161
Cdd:PHA03095  132 PKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADVYAVDDRFRSLLHHhlqSFKPRARIVRE-LIR 210

                          90       100
                  ....*....|....*....|....*....
gi 1134612274 162 HDADINAQTKGLLTPLHLAAGNRDSRDTL 190
Cdd:PHA03095  211 AGCDPAATDMLGNTPLHSMATGSSCKRSL 239
Ank_4 pfam13637
Ankyrin repeats (many copies);
140-194 9.02e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.35  E-value: 9.02e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1134612274 140 GWTPLHSACKWNNTKVASFLLQHDADINAQTKGLLTPLHLAAGNRDSrDTLELLL 194
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNV-EVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 82-211 5.16e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 52.75  E-value: 5.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134612274  82 EKNRLATVQRL--LSEKAAEVNTRDEDEYTPLHRAAYSGHIDVVRELVAKGADVHAVTVDGWTPLHSACKW-----NNTK 154
Cdd:PHA03100    8 TKSRIIKVKNIkyIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIkynltDVKE 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1134612274 155 VASFLLQHDADINAQTKGLLTPLHLAAGNR-DSRDTLELLLMNRyIKPELKNNSQETA 211
Cdd:PHA03100   88 IVKLLLEYGANVNAPDNNGITPLLYAISKKsNSYSIVEYLLDNG-ANVNIKNSDGENL 144
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 115-194 7.31e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.59  E-value: 7.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134612274 115 AYSGHIDVVRELVAKGADVHAVTVDGWTPLHSACKWNNTKVASFLLQHDADINAQTKGLLTPLHLAAGNrDSRDTLELLL 194
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEEN-GFREVVQLLS 168
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 76-223 9.49e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 51.99  E-value: 9.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134612274  76 LLLWAAEKNRLATVQRLLSEKAAEVNTRDEDEYTPLHRAAYSGHID-VVRELVAKGADVHAVTVDGWTPLHSACKWN-NT 153
Cdd:PHA02876  242 LSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGyDT 321

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134612274 154 KVASFLLQHDADINAQTKGLLTPLHLAAGNRDSRDTLELLLmnryikpELKNNSQetASDIARRTSIyHY 223
Cdd:PHA02876  322 ENIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIVITLL-------ELGANVN--ARDYCDKTPI-HY 381
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 89-192 1.48e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 51.60  E-value: 1.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134612274  89 VQRLLSEKAAEVNTRDEDEYTPLHRAAYSGHIDVVRELVAKGADVHAVTVDGWTPLHSACKWNNTKVASFLLQHDADINA 168
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINK 239

                          90       100
                  ....*....|....*....|....
gi 1134612274 169 QTKGLLTplhlAAGNRDSRDTLEL 192
Cdd:PHA02876  240 NDLSLLK----AIRNEDLETSLLL 259
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 81-197 2.38e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 50.76  E-value: 2.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134612274  81 AEKNRLATVQRLLSEKAAEVNTRDEDEYTPLHRAAYSGHIDVVRELVAKGADVHAVTV-DGWTPLHSACKWNNTKVASFL 159
Cdd:PHA02875   42 AMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYkDGMTPLHLATILKKLDIMKLL 121

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1134612274 160 LQHDADINAQTKGLLTPLHLAAGNRDSRDTlELLLMNR 197
Cdd:PHA02875  122 IARGADPDIPNTDKFSPLHLAVMMGDIKGI-ELLIDHK 158
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 80-185 2.78e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 50.37  E-value: 2.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134612274  80 AAEKNRLATVQRLLSEKAAEVNTRDEDEYTPLHRAAYSGHIDVVRELVAKGADVHAVTVDGWTPLHSACKWNNTKVASFL 159
Cdd:PHA02875   75 AVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELL 154

                          90       100
                  ....*....|....*....|....*.
gi 1134612274 160 LQHDADINAQTKGLLTPLHLAAGNRD 185
Cdd:PHA02875  155 IDHKACLDIEDCCGCTPLIIAMAKGD 180
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 91-180 5.44e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 50.06  E-value: 5.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134612274  91 RLLSEKAAEVNTRDEDEYTPLHRAA-YSGHIDVVRELVAKGADVHAVTVDGWTPLHSACKWNNTKVASFLLQHDADINAQ 169
Cdd:PHA02876  325 RTLIMLGADVNAADRLYITPLHQAStLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEAL 404

                          90
                  ....*....|.
gi 1134612274 170 TKGLLTPLHLA 180
Cdd:PHA02876  405 SQKIGTALHFA 415
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 139-171 6.60e-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: 6.60e-07
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1134612274 139 DGWTPLHSAC-KWNNTKVASFLLQHDADINAQTK 171
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 77-181 7.64e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 49.29  E-value: 7.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134612274  77 LLWAAEKNRLATVQRLLSEKAAEVNTRDEDEYTPLHRAAYSGH-IDVVRELVAKGADVHAVTVDGWTPLHSACKWNNTK- 154
Cdd:PHA02876  277 LHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKd 356

                          90       100
                  ....*....|....*....|....*..
gi 1134612274 155 VASFLLQHDADINAQTKGLLTPLHLAA 181
Cdd:PHA02876  357 IVITLLELGANVNARDYCDKTPIHYAA 383
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 139-168 1.34e-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: 43.79  E-value: 1.34e-06
                          10        20        30
                  ....*....|....*....|....*....|
gi 1134612274 139 DGWTPLHSACKWNNTKVASFLLQHDADINA 168
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 139-168 1.48e-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: 43.73  E-value: 1.48e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 1134612274  139 DGWTPLHSACKWNNTKVASFLLQHDADINA 168
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 77-174 4.14e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 46.97  E-value: 4.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134612274  77 LLWAAEKNRLATVQRLLsEKAAEVNTRDEDEYTPLHRAAYSGHIDVVRELVAKGADVhavtvdgwtplhsackwnNTKVA 156
Cdd:PHA03100  196 LHYAVYNNNPEFVKYLL-DLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSI------------------KTIIE 256

                          90
                  ....*....|....*...
gi 1134612274 157 SFLLQHDADINAQTKGLL 174
Cdd:PHA03100  257 TLLYFKDKDLNTITKIKM 274
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 106-135 4.85e-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: 4.85e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 1134612274  106 DEYTPLHRAAYSGHIDVVRELVAKGADVHA 135
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 62-179 5.98e-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: 46.54  E-value: 5.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134612274  62 YQLQEKKMEKDPsklLLWAAEKNRLATVQRLLSEKAAEVNTR--------------DEDE-------------------- 107
Cdd:cd22192     9 HLLQQKRISESP---LLLAAKENDVQAIKKLLKCPSCDLFQRgalgetalhvaalyDNLEaavvlmeaapelvnepmtsd 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134612274 108 -Y---TPLHRAAYSGHIDVVRELVAKGADV--------------HAVTVDGWTPLHSACKWNNTKVASFLLQHDADINAQ 169
Cdd:cd22192    86 lYqgeTALHIAVVNQNLNLVRELIARGADVvspratgtffrpgpKNLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQ 165

                         170
                  ....*....|
gi 1134612274 170 TKGLLTPLHL 179
Cdd:cd22192   166 DSLGNTVLHI 175
PHA02798 PHA02798
ankyrin-like protein; Provisional
 91-194 7.63e-06

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 46.37  E-value: 7.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134612274  91 RLLSEKAAEVNTRDEDEYTPL-----HRAAYSGHIDVVRELVAKGADVHAVTVDGWTPLH---SACKWNNTKVASFLLQH 162
Cdd:PHA02798   55 KLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYcllSNGYINNLEILLFMIEN 134

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1134612274 163 DADINAQTKGLLTPL--HLAAGNRDSRDTLELLL 194
Cdd:PHA02798  135 GADTTLLDKDGFTMLqvYLQSNHHIDIEIIKLLL 168
PHA02946 PHA02946
ankyin-like protein; Provisional
 123-185 8.95e-06

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 46.20  E-value: 8.95e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1134612274 123 VRELVAKGADVHAVTVDGWTPLHSACKWNNTKVASFLLQHDADINAQTKGLLTPLHLAAGNRD 185
Cdd:PHA02946   55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDD 117
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 106-137 9.47e-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: 9.47e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1134612274 106 DEYTPLHRAAYS-GHIDVVRELVAKGADVHAVT 137
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 106-135 1.77e-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: 40.70  E-value: 1.77e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 1134612274 106 DEYTPLHRAAYSGHIDVVRELVAKGADVHA 135
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
126-180 2.49e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.79  E-value: 2.49e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1134612274 126 LVAKG-ADVHAVTVDGWTPLHSACKWNNTKVASFLLQHDADINAQTKGLLTPLHLA 180
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 78-167 8.54e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 43.06  E-value: 8.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134612274  78 LWAAEKNRLATVQRLLSEKAAEVNTRDEDEYTPLHRAAYSGHIDVVRELVAKGADVHAVTVDGWTPLHSACKWNNTKVAS 157
Cdd:PHA02875  106 LHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICK 185

                          90
                  ....*....|
gi 1134612274 158 FLLQHDADIN 167
Cdd:PHA02875  186 MLLDSGANID 195
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 76-144 1.08e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 42.93  E-value: 1.08e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134612274  76 LLLWAAEKNRLATVQRLLsEKAAEVNTRDEDEYTPLHRAAYSGHIDVVRELVAKGADV-HAVTVDGWTPL 144
Cdd:PLN03192  625 LLCTAAKRNDLTAMKELL-KQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVdKANTDDDFSPT 693
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 114-199 1.15e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 42.67  E-value: 1.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134612274 114 AAYSGHIDVVRELVAKGADVHAVTVDGWTPLHSACKWNNTKVASFLLQHDADINAQTKGLLTPLHLAAGNRDSRDTLELL 193
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88


                  ....*.
gi 1134612274 194 LMNRYI 199
Cdd:PHA02875   89 DLGKFA 94
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 64-198 4.01e-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: 41.22  E-value: 4.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134612274  64 LQEKKMEKDPSKLLLWAAEKNRLATVQRLLS--EKAAE-------VNTRDEDEY----TPLHRAAYSGHIDVVRELVAKG 130
Cdd:TIGR00870  72 LLNLSCRGAVGDTLLHAISLEYVDAVEAILLhlLAAFRksgplelANDQYTSEFtpgiTALHLAAHRQNYEIVKLLLERG 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134612274 131 ADVHA-------VTVDGWT-------PLHSACKWNNTKVASFLLQHDADINAQTKGLLTPLHLAAGNRDSRDTLELLLMN 196
Cdd:TIGR00870 152 ASVPAracgdffVKSQGVDsfyhgesPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVMENEFKAEYEELSCQ 231


                  ..
gi 1134612274 197 RY 198
Cdd:TIGR00870 232 MY 233
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 91-166 4.42e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 41.20  E-value: 4.42e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1134612274  91 RLLSEKAAEVNTRDEDEYTPLHRAAYSG-HIDVVRELVAKGADVHAVTVDGWTPLHSACKWNNtkVASFLLQHDADI 166
Cdd:PHA02876  426 KTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIALEYHG--IVNILLHYGAEL 500
PHA02795 PHA02795
ankyrin-like protein; Provisional
 99-147 4.64e-04

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 40.75  E-value: 4.64e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1134612274  99 EVNTRDEDEYTPLHRAAYSGHIDVVRELVAKGADVHAVTVDGWTPLHSA 147
Cdd:PHA02795  213 DINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVA 261
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 110-226 4.73e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 40.63  E-value: 4.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134612274 110 PLHRAAYSGHIDVVRELVAKGADVHAVTVDGWTPLHSACKWNN------------------------------------- 152
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNklgmkemirsinkcsvfytlvaikdafnnrnveifki 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134612274 153 ---------------------------TKVASFLLQHDADINAQTKGLL-TPLHLAAGNRDSRDTLELLLMNRYIK-PEL 203
Cdd:PHA02878  120 iltnrykniqtidlvyidkkskddiieAEITKLLLSYGADINMKDRHKGnTALHYATENKDQRLTELLLSYGANVNiPDK 199

                         170       180
                  ....*....|....*....|...
gi 1134612274 204 KNNSQETASDIARRTSIYHYLFE 226
Cdd:PHA02878  200 TNNSPLHHAVKHYNKPIVHILLE 222
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 86-165 1.51e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 39.18  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134612274  86 LATVQRLLSEKAAEVNTRDEDEYTPLHRAAYSGHIDVVRELVAKGADVHAVTVDGWTPLHSACKWNNTKVASFLLQHDAD 165
Cdd:PHA02874   14 IEAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVD 93
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 91-159 1.68e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 37.93  E-value: 1.68e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1134612274  91 RLLSEKAAEVNTRDE-DEYTPLHRAAYSGHIDVVRELVAK-GADVHAVTVDGWTPLHSACKWNNTKVASFL 159
Cdd:PHA02736   75 KLLMEWGADINGKERvFGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERHDAKMMNIL 145
Ank_5 pfam13857
Ankyrin repeats (many copies);
159-215 3.35e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.01  E-value: 3.35e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1134612274 159 LLQHD-ADINAQTKGLLTPLHLAAGNRDSRDtLELLLMNRYiKPELKNNSQETASDIA 215
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEI-VRVLLAYGV-DLNLKDEEGLTALDLA 56
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 116-196 3.52e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 38.02  E-value: 3.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134612274 116 YSGHIDVVRELVAKGADVHAVTVD-GWTPLHSACKWNNTKVASFLLQHDADINAQTKGLLTPLhLAAGNRDSRDTLELLL 194
Cdd:PHA02874   10 YSGDIEAIEKIIKNKGNCINISVDeTTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPL-LTAIKIGAHDIIKLLI 88


                  ..
gi 1134612274 195 MN 196
Cdd:PHA02874   89 DN 90
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 109-227 6.40e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 36.88  E-value: 6.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134612274 109 TPLHRAAYSGHIDVVRELVAKGADVHAVTVDG-WTPLHSACKWNNTKVASFLLQHDADINAQTKGLLTPLHLAagnrdsr 187
Cdd:PHA02884   72 NPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAkITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELA------- 144

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1134612274 188 dtleLLLMNRYIKPELKNNsqeTASDIARRTSIYHYLFEI 227
Cdd:PHA02884  145 ----LMICNNFLAFMICDN---EISNFYKHPKKILINFDI 177
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 124-187 6.91e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 36.01  E-value: 6.91e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1134612274 124 RELVAKGADVHAV-TVDGWTPLHSACKWNNTKVASFLL-QHDADINAQTKGLLTPLHLAAGNRDSR 187
Cdd:PHA02736   75 KLLMEWGADINGKeRVFGNTPLHIAVYTQNYELATWLCnQPGVNMEILNYAFKTPYYVACERHDAK 140
 
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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