NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|22165398|ref|NP_062657|]
View 

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

 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];
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 22165398  76 LLLWAAEKNRLATVQRLLsEKAAEVNTRDEDEYTPLHRAAYSGHIDVVRELVAKGADVHAVTVDGWTPLHSACKWNNTKV 155
Cdd:COG0666  90 LLHAAARNGDLEIVKLLL-EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEI 168

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22165398 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 22165398  76 LLLWAAEKNRLATVQRLLsEKAAEVNTRDEDEYTPLHRAAYSGHIDVVRELVAKGADVHAVTVDGWTPLHSACKWNNTKV 155
Cdd:COG0666  90 LLHAAARNGDLEIVKLLL-EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEI 168

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22165398 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 22165398    77 LLWAAEKNRLATVQRLLSEKAaEVNTRDEDEYTPLHRAAYSGHIDVVRELVAKgADVhAVTVDGWTPLHSACKWNNTKVA 156
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGA-DANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADV-NLKDNGRTALHYAARSGHLEIV 77

                          90
                  ....*....|...
gi 22165398   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 22165398   89 VQRLLSEKAAEVNTRDEDEYTPLHRAAYSGH-IDVVRELVAKGADVHAVTVDGWTPLHSAC--KWNNTKVASFLLQHDAD 165
Cdd:PHA03095  65 IVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGADVNAKDKVGRTPLHVYLsgFNINPKVIRLLLRKGAD 144

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 22165398  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 22165398    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 22165398  62 YQLQEKKMEKDPsklLLWAAEKNRLATVQRLLSEKAAEVNTR--------------DEDE-------------------- 107
Cdd:cd22192   9 HLLQQKRISESP---LLLAAKENDVQAIKKLLKCPSCDLFQRgalgetalhvaalyDNLEaavvlmeaapelvnepmtsd 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22165398 108 -Y---TPLHRAAYSGHIDVVRELVAKGADV--------------HAVTVDGWTPLHSACKWNNTKVASFLLQHDADINAQ 169
Cdd:cd22192  86 lYqgeTALHIAVVNQNLNLVRELIARGADVvspratgtffrpgpKNLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQ 165

                       170
                ....*....|
gi 22165398 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 22165398    64 LQEKKMEKDPSKLLLWAAEKNRLATVQRLLS--EKAAE-------VNTRDEDEY----TPLHRAAYSGHIDVVRELVAKG 130
Cdd:TIGR00870  72 LLNLSCRGAVGDTLLHAISLEYVDAVEAILLhlLAAFRksgplelANDQYTSEFtpgiTALHLAAHRQNYEIVKLLLERG 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22165398   131 ADVHA-------VTVDGWT-------PLHSACKWNNTKVASFLLQHDADINAQTKGLLTPLHLAAGNRDSRDTLELLLMN 196
Cdd:TIGR00870 152 ASVPAracgdffVKSQGVDsfyhgesPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVMENEFKAEYEELSCQ 231


                  ..
gi 22165398   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 22165398  76 LLLWAAEKNRLATVQRLLsEKAAEVNTRDEDEYTPLHRAAYSGHIDVVRELVAKGADVHAVTVDGWTPLHSACKWNNTKV 155
Cdd:COG0666  90 LLHAAARNGDLEIVKLLL-EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEI 168

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22165398 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 22165398  76 LLLWAAEKNRLATVQRLLsEKAAEVNTRDEDEYTPLHRAAYSGHIDVVRELVAKGADVHAVTVDGWTPLHSACKWNNTKV 155
Cdd:COG0666 123 PLHLAAYNGNLEIVKLLL-EAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEI 201

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22165398 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 22165398  71 KDPSKLLLWAAEKNRLATVQRLLSEKAAEVNTRDEDEYTPLHRAAYSGHIDVVRELVAKGADVHAVTVDGWTPLHSACKW 150
Cdd:COG0666  51 DALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYN 130

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22165398 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 22165398  76 LLLWAAEKNRLATVQRLLsEKAAEVNTRDEDEYTPLHRAAYSGHIDVVRELVAKGADVHAVTVDGWTPLHSACKWNNTKV 155
Cdd:COG0666 156 PLHLAAANGNLEIVKLLL-EAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI 234

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 22165398 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 22165398    77 LLWAAEKNRLATVQRLLSEKAaEVNTRDEDEYTPLHRAAYSGHIDVVRELVAKgADVhAVTVDGWTPLHSACKWNNTKVA 156
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGA-DANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADV-NLKDNGRTALHYAARSGHLEIV 77

                          90
                  ....*....|...
gi 22165398   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 22165398   111 LHRAAYSGHIDVVRELVAKGADVHAVTVDGWTPLHSACKWNNTKVASFLLQHdADINAQTKGlLTPLHLAAGNRdSRDTL 190
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG-RTALHYAARSG-HLEIV 77

                          90
                  ....*....|....*
gi 22165398   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 22165398  76 LLLWAAEKNRLATVQRLLSEKAAEVNTRDEDEYTPLHRAAYSGHIDVVRELVAKGADVHAVTVDGWTPLHSACKWNNTKV 155
Cdd:COG0666  23 LLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEI 102

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 22165398 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 22165398   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 22165398   89 VQRLLSEKAAEVNTRDEDEYTPLHRAAYSGH-IDVVRELVAKGADVHAVTVDGWTPLHSAC--KWNNTKVASFLLQHDAD 165
Cdd:PHA03095  65 IVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGADVNAKDKVGRTPLHVYLsgFNINPKVIRLLLRKGAD 144

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 22165398  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 22165398   81 AEKNRLATVQRLLSeKAAEVNTRDEDEYTPLH---RAAYSGHIDVVRELVAKGADVHAVTVDGWTPLHSACKWNNT-KVA 156
Cdd:PHA03095  22 ASNVTVEEVRRLLA-AGADVNFRGEYGKTPLHlylHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVI 100

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 22165398  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 22165398   83 KNRlatVQRLLSeKAAEVNTRDEDEYTPLHRAAYSGHIDVVRELVAKGADVHAVTVDGWTPLHSACKWNNTKVASFLLQH 162
Cdd:PHA03100 172 KNR---VNYLLS-YGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNN 247


                 ....*.
gi 22165398  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 22165398   76 LLLWAAEKNRLATVQRLLsEKAAEVNTRDEDEYTPLHRAAYSGHIDVVRELVAKGADVHAVTVDGWTPLHSACKWNNTKV 155
Cdd:PHA02874 127 FLHYAIKKGDLESIKMLF-EYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYAC 205

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22165398  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 22165398   87 ATVQRLLSEKAAEVNTRDEDE-YTPLHRAAYSGHIDVVRELVAKGADVHAVTVDGWTPLHSACKWNNTKVASFLLQHDAD 165
Cdd:PHA02878 147 AEITKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS 226

                         90       100
                 ....*....|....*....|....*....
gi 22165398  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 22165398  77 LLWAAEKNRLATVQRLLsEKAAEVNTRDEDEYTPLHRAAYSGHIDVVRELVAKGADVHAVTVDGWTPLHSACKWNNTKVA 156
Cdd:COG0666 190 LHLAAENGHLEIVKLLL-EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIV 268

                        90       100
                ....*....|....*....|.
gi 22165398 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 22165398   93 LSEKAAEVNTRDEDEYTPLHRAAYSGHIDVVRELVAKGADVHAVTVDGWTPLHSA-CKWNNTKVASFLLQHDADINAQTK 171
Cdd:PHA02876 361 LLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNK 440

                         90       100
                 ....*....|....*....|....*
gi 22165398  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 22165398   67 KKMEKDPSKLLLWAAEKNRLATVQRLLSEKAAEVNTRDEDEYTPLHRAAYSGHIDVVRELVAKGADVHAVTVDGWTPLH- 145
Cdd:PHA02878 161 NMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHi 240

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 22165398  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 22165398   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 22165398   81 AEKNRLATVQRLLSEKAAEVNTRDEDEYTPLHRAAYSGHIDVVRELVAKGADVHAVTVDGWTPLHSACKWNNTKVAsfLL 160
Cdd:PHA02874 164 AIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIE--LL 241

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 22165398  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 22165398    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 22165398   76 LLLWAAEKNRLATVQRLLSEKAAEVNTRDEDEYTPLHRAAYSGHID--VVRELVAKGADVHAVT-VD------------- 139
Cdd:PHA03100 110 LLYAISKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDINAKNrVNyllsygvpinikd 189

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 22165398  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 22165398   78 LWAAEKNRLATVQRLLSEKAAEVNTRDEDEYTPLHRA-AYSGHIDVVRELVAKGADVHA-VTVDGWTPLHSACKwnNTKV 155
Cdd:PHA02878 205 LHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAkSYILGLTALHSSIK--SERK 282

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 22165398  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 22165398    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 22165398   87 ATVQRLLSEKAAEVNTRDEDEYTPLHRAAY--SGHIDVVRELVAKGADVHAVTVDGWTPLHSACKWNNTKVASFLLQHDA 164
Cdd:PHA03095 202 ARIVRELIRAGCDPAATDMLGNTPLHSMATgsSCKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGA 281

                         90       100
                 ....*....|....*....|...
gi 22165398  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 22165398   87 ATVQRLLSEKAAEVNTRDEDEYTPLHRAAYSGHIDV--VRELVAKGADVHAVTVDGWTPLHS---ACKWNNTKVASfLLQ 161
Cdd:PHA03095 132 PKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADVYAVDDRFRSLLHHhlqSFKPRARIVRE-LIR 210

                         90       100
                 ....*....|....*....|....*....
gi 22165398  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 22165398   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 22165398   82 EKNRLATVQRL--LSEKAAEVNTRDEDEYTPLHRAAYSGHIDVVRELVAKGADVHAVTVDGWTPLHSACKW-----NNTK 154
Cdd:PHA03100   8 TKSRIIKVKNIkyIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIkynltDVKE 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 22165398  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 22165398  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 22165398   76 LLLWAAEKNRLATVQRLLSEKAAEVNTRDEDEYTPLHRAAYSGHID-VVRELVAKGADVHAVTVDGWTPLHSACKWN-NT 153
Cdd:PHA02876 242 LSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGyDT 321

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22165398  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 22165398   89 VQRLLSEKAAEVNTRDEDEYTPLHRAAYSGHIDVVRELVAKGADVHAVTVDGWTPLHSACKWNNTKVASFLLQHDADINA 168
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINK 239

                         90       100
                 ....*....|....*....|....
gi 22165398  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 22165398   81 AEKNRLATVQRLLSEKAAEVNTRDEDEYTPLHRAAYSGHIDVVRELVAKGADVHAVTV-DGWTPLHSACKWNNTKVASFL 159
Cdd:PHA02875  42 AMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYkDGMTPLHLATILKKLDIMKLL 121

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 22165398  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 22165398   80 AAEKNRLATVQRLLSEKAAEVNTRDEDEYTPLHRAAYSGHIDVVRELVAKGADVHAVTVDGWTPLHSACKWNNTKVASFL 159
Cdd:PHA02875  75 AVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELL 154

                         90       100
                 ....*....|....*....|....*.
gi 22165398  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 22165398   91 RLLSEKAAEVNTRDEDEYTPLHRAA-YSGHIDVVRELVAKGADVHAVTVDGWTPLHSACKWNNTKVASFLLQHDADINAQ 169
Cdd:PHA02876 325 RTLIMLGADVNAADRLYITPLHQAStLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEAL 404

                         90
                 ....*....|.
gi 22165398  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 22165398   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 22165398   77 LLWAAEKNRLATVQRLLSEKAAEVNTRDEDEYTPLHRAAYSGH-IDVVRELVAKGADVHAVTVDGWTPLHSACKWNNTK- 154
Cdd:PHA02876 277 LHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKd 356

                         90       100
                 ....*....|....*....|....*..
gi 22165398  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 22165398   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 22165398    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 22165398   77 LLWAAEKNRLATVQRLLsEKAAEVNTRDEDEYTPLHRAAYSGHIDVVRELVAKGADVhavtvdgwtplhsackwnNTKVA 156
Cdd:PHA03100 196 LHYAVYNNNPEFVKYLL-DLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSI------------------KTIIE 256

                         90
                 ....*....|....*...
gi 22165398  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 22165398    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 22165398  62 YQLQEKKMEKDPsklLLWAAEKNRLATVQRLLSEKAAEVNTR--------------DEDE-------------------- 107
Cdd:cd22192   9 HLLQQKRISESP---LLLAAKENDVQAIKKLLKCPSCDLFQRgalgetalhvaalyDNLEaavvlmeaapelvnepmtsd 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22165398 108 -Y---TPLHRAAYSGHIDVVRELVAKGADV--------------HAVTVDGWTPLHSACKWNNTKVASFLLQHDADINAQ 169
Cdd:cd22192  86 lYqgeTALHIAVVNQNLNLVRELIARGADVvspratgtffrpgpKNLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQ 165

                       170
                ....*....|
gi 22165398 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 22165398   91 RLLSEKAAEVNTRDEDEYTPL-----HRAAYSGHIDVVRELVAKGADVHAVTVDGWTPLH---SACKWNNTKVASFLLQH 162
Cdd:PHA02798  55 KLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYcllSNGYINNLEILLFMIEN 134

                         90       100       110
                 ....*....|....*....|....*....|....
gi 22165398  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 22165398  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 22165398   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 22165398   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 22165398   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 22165398   78 LWAAEKNRLATVQRLLSEKAAEVNTRDEDEYTPLHRAAYSGHIDVVRELVAKGADVHAVTVDGWTPLHSACKWNNTKVAS 157
Cdd:PHA02875 106 LHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICK 185

                         90
                 ....*....|
gi 22165398  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 22165398   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 22165398  114 AAYSGHIDVVRELVAKGADVHAVTVDGWTPLHSACKWNNTKVASFLLQHDADINAQTKGLLTPLHLAAGNRDSRDTLELL 193
Cdd:PHA02875   9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88


                 ....*.
gi 22165398  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 22165398    64 LQEKKMEKDPSKLLLWAAEKNRLATVQRLLS--EKAAE-------VNTRDEDEY----TPLHRAAYSGHIDVVRELVAKG 130
Cdd:TIGR00870  72 LLNLSCRGAVGDTLLHAISLEYVDAVEAILLhlLAAFRksgplelANDQYTSEFtpgiTALHLAAHRQNYEIVKLLLERG 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22165398   131 ADVHA-------VTVDGWT-------PLHSACKWNNTKVASFLLQHDADINAQTKGLLTPLHLAAGNRDSRDTLELLLMN 196
Cdd:TIGR00870 152 ASVPAracgdffVKSQGVDsfyhgesPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVMENEFKAEYEELSCQ 231


                  ..
gi 22165398   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 22165398   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 22165398   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 22165398  110 PLHRAAYSGHIDVVRELVAKGADVHAVTVDGWTPLHSACKWNN------------------------------------- 152
Cdd:PHA02878  40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNklgmkemirsinkcsvfytlvaikdafnnrnveifki 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22165398  153 ---------------------------TKVASFLLQHDADINAQTKGLL-TPLHLAAGNRDSRDTLELLLMNRYIK-PEL 203
Cdd:PHA02878 120 iltnrykniqtidlvyidkkskddiieAEITKLLLSYGADINMKDRHKGnTALHYATENKDQRLTELLLSYGANVNiPDK 199

                        170       180
                 ....*....|....*....|...
gi 22165398  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 22165398   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 22165398   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 22165398   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 22165398  116 YSGHIDVVRELVAKGADVHAVTVD-GWTPLHSACKWNNTKVASFLLQHDADINAQTKGLLTPLhLAAGNRDSRDTLELLL 194
Cdd:PHA02874  10 YSGDIEAIEKIIKNKGNCINISVDeTTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPL-LTAIKIGAHDIIKLLI 88


                 ..
gi 22165398  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 22165398  109 TPLHRAAYSGHIDVVRELVAKGADVHAVTVDG-WTPLHSACKWNNTKVASFLLQHDADINAQTKGLLTPLHLAagnrdsr 187
Cdd:PHA02884  72 NPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAkITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELA------- 144

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 22165398  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 22165398  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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH