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Conserved domains on  [gi|30684671|ref|NP_193650|]
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Ankyrin repeat family protein [Arabidopsis thaliana]

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];
20-179 2.14e-34

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 124.68  E-value: 2.14e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684671  20 LHSAARSGDLAAVQSIISsNPLAVNSRDKHSRTPLHLAAWAGHNEVVSYLCKNKADVGAAAGDDMGAIHFASQKGHLEVV 99
Cdd:COG0666  91 LHAAARNGDLEIVKLLLE-AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684671 100 RTLLSAGGSVKSITRKGLTPLHYAAQGSHFEIVKYLVKKGASVRATTKAGKSPADVAGNAETQNFLEECEEQARKAKVNN 179
Cdd:COG0666 170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKD 249
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
20-179 2.14e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 124.68  E-value: 2.14e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684671  20 LHSAARSGDLAAVQSIISsNPLAVNSRDKHSRTPLHLAAWAGHNEVVSYLCKNKADVGAAAGDDMGAIHFASQKGHLEVV 99
Cdd:COG0666  91 LHAAARNGDLEIVKLLLE-AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684671 100 RTLLSAGGSVKSITRKGLTPLHYAAQGSHFEIVKYLVKKGASVRATTKAGKSPADVAGNAETQNFLEECEEQARKAKVNN 179
Cdd:COG0666 170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKD 249
Ank_2 pfam12796
Ankyrin repeats (3 copies);
54-145 6.57e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 83.63  E-value: 6.57e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684671    54 LHLAAWAGHNEVVSYLCKNKADVGAAAGDDMGAIHFASQKGHLEVVRTLLSAGgsVKSITRKGLTPLHYAAQGSHFEIVK 133
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA--DVNLKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 30684671   134 YLVKKGASVRAT 145
Cdd:pfam12796  79 LLLEKGADINVK 90
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 35-167 1.83e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 72.01  E-value: 1.83e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684671   35 IISSNPLAVNSRDKHSRTPLHLAAWA--GHNEVVSYLCKNKADVGAAAGDDMGAIHFASQKGH--LEVVRTLLSAGGSVK 110
Cdd:PHA03100  91 LLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDIN 170

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30684671  111 SITR----------------KGLTPLHYAAQGSHFEIVKYLVKKGASVRATTKAGKSPADVAGNAETQNFLEE 167
Cdd:PHA03100 171 AKNRvnyllsygvpinikdvYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKL 243
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 23-144 5.08e-08

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: 53.09  E-value: 5.08e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684671  23 AARSGDLAAVQSIISSNPLAVNSRDKHSRTPLHLAAWAGHNEVVSYLCKNKAD-VGAAAGDDM----GAIHFASQKGHLE 97
Cdd:cd22192  24 AAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPMTSDLyqgeTALHIAVVNQNLN 103

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30684671  98 VVRTLLSAGGSVKS---------ITRKGLT-----PLHYAAQGSHFEIVKYLVKKGASVRA 144
Cdd:cd22192 104 LVRELIARGADVVSpratgtffrPGPKNLIyygehPLSFAACVGNEEIVRLLIEHGADIRA 164
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 115-142 1.47e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 40.65  E-value: 1.47e-05
                           10        20
                   ....*....|....*....|....*...
gi 30684671    115 KGLTPLHYAAQGSHFEIVKYLVKKGASV 142
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 22-145 9.41e-04

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 40.06  E-value: 9.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684671    22 SAARSGDLAAVQSII-SSNPLAVNSRDKHSRTPLHLAAWAGHN-EVVSYLCKNKADVgaAAGDdmGAIHFASqKGHLEVV 99
Cdd:TIGR00870  23 PAAERGDLASVYRDLeEPKKLNINCPDRLGRSALFVAAIENENlELTELLLNLSCRG--AVGD--TLLHAIS-LEYVDAV 97

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684671   100 RTLLS-----AGGSV---------KSITRKGLTPLHYAAQGSHFEIVKYLVKKGASVRAT 145
Cdd:TIGR00870  98 EAILLhllaaFRKSGplelandqyTSEFTPGITALHLAAHRQNYEIVKLLLERGASVPAR 157
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
20-179 2.14e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 124.68  E-value: 2.14e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684671  20 LHSAARSGDLAAVQSIISsNPLAVNSRDKHSRTPLHLAAWAGHNEVVSYLCKNKADVGAAAGDDMGAIHFASQKGHLEVV 99
Cdd:COG0666  91 LHAAARNGDLEIVKLLLE-AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684671 100 RTLLSAGGSVKSITRKGLTPLHYAAQGSHFEIVKYLVKKGASVRATTKAGKSPADVAGNAETQNFLEECEEQARKAKVNN 179
Cdd:COG0666 170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKD 249
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
20-185 1.16e-27

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 106.96  E-value: 1.16e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684671  20 LHSAARSGDLAAVQSIISSNpLAVNSRDKHSRTPLHLAAWAGHNEVVSYLCKNKADVGAAAGDDMGAIHFASQKGHLEVV 99
Cdd:COG0666 124 LHLAAYNGNLEIVKLLLEAG-ADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684671 100 RTLLSAGGSVKSITRKGLTPLHYAAQGSHFEIVKYLVKKGASVRATTKAGKSPADVAGNAETQNFLEECEEQARKAKVNN 179
Cdd:COG0666 203 KLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282


                ....*.
gi 30684671 180 EKKTEI 185
Cdd:COG0666 283 LDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
19-179 1.93e-27

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 106.58  E-value: 1.93e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684671  19 DLHSAARSGDLAAVQSIISSNPLAVNSRDKHSRTPLHLAAWAGHNEVVSYLCKNKADVGAAAGDDMGAIHFASQKGHLEV 98
Cdd:COG0666  56 LLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI 135

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684671  99 VRTLLSAGGSVKSITRKGLTPLHYAAQGSHFEIVKYLVKKGASVRATTKAGKSPADVA---GNAETQNFLEEceeqaRKA 175
Cdd:COG0666 136 VKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAaenGHLEIVKLLLE-----AGA 210


                ....
gi 30684671 176 KVNN 179
Cdd:COG0666 211 DVNA 214
Ank_2 pfam12796
Ankyrin repeats (3 copies);
54-145 6.57e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 83.63  E-value: 6.57e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684671    54 LHLAAWAGHNEVVSYLCKNKADVGAAAGDDMGAIHFASQKGHLEVVRTLLSAGgsVKSITRKGLTPLHYAAQGSHFEIVK 133
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA--DVNLKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 30684671   134 YLVKKGASVRAT 145
Cdd:pfam12796  79 LLLEKGADINVK 90
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
20-161 9.77e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 80.38  E-value: 9.77e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684671  20 LHSAARSGDLAAVQSIISSNPLAVNSRDKHSRTPLHLAAWAGHNEVVSYLCKNKADVGAAAGDDMGAIHFASQKGHLEVV 99
Cdd:COG0666  24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIV 103

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30684671 100 RTLLSAGGSVKSITRKGLTPLHYAAQGSHFEIVKYLVKKGASVRATTKAGKSPADVA---GNAET 161
Cdd:COG0666 104 KLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAaanGNLEI 168
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 35-167 1.83e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 72.01  E-value: 1.83e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684671   35 IISSNPLAVNSRDKHSRTPLHLAAWA--GHNEVVSYLCKNKADVGAAAGDDMGAIHFASQKGH--LEVVRTLLSAGGSVK 110
Cdd:PHA03100  91 LLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDIN 170

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30684671  111 SITR----------------KGLTPLHYAAQGSHFEIVKYLVKKGASVRATTKAGKSPADVAGNAETQNFLEE 167
Cdd:PHA03100 171 AKNRvnyllsygvpinikdvYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKL 243
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 36-152 1.76e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 68.92  E-value: 1.76e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684671   36 ISSNPLAVNSRDKHSRTPLHLAAWAGHNEVVSYLCKNKADVGAAAGDDMGAIHFASQKGH-----LEVVRTLLSAGGSVK 110
Cdd:PHA03100  21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVN 100

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 30684671  111 SITRKGLTPLHYAAQGS--HFEIVKYLVKKGASVRATTKAGKSP 152
Cdd:PHA03100 101 APDNNGITPLLYAISKKsnSYSIVEYLLDNGANVNIKNSDGENL 144
Ank_2 pfam12796
Ankyrin repeats (3 copies);
87-156 5.63e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.83  E-value: 5.63e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684671    87 IHFASQKGHLEVVRTLLSAGGSVKSITRKGLTPLHYAAQGSHFEIVKYLVKKgASVRATTKaGKSPADVA 156
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYA 68
Ank_4 pfam13637
Ankyrin repeats (many copies);
84-136 3.25e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.90  E-value: 3.25e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 30684671    84 MGAIHFASQKGHLEVVRTLLSAGGSVKSITRKGLTPLHYAAQGSHFEIVKYLV 136
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 32-152 3.29e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 62.29  E-value: 3.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684671   32 VQSIISSNpLAVNSRDKHSRTPLHLAAWAGHNEVVSYLCKNKADVGAAagDDMG--AIHFASQKGHLEVVRTLLSAGGSV 109
Cdd:PHA02874 107 IKTILDCG-IDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIE--DDNGcyPIHIAIKHNFFDIIKLLLEKGAYA 183

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 30684671  110 KSITRKGLTPLHYAAQGSHFEIVKYLVKKGASVRATTKAGKSP 152
Cdd:PHA02874 184 NVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTP 226
PHA03095 PHA03095
ankyrin-like protein; Provisional
 43-165 4.67e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 58.88  E-value: 4.67e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684671   43 VNSRDKHSRTPLH-LAAWAGHN--EVVSYLCKNKADVGAAAGDDMGAIH-FASQKGHLEVVRTLLSAGGSVKSITRKGLT 118
Cdd:PHA03095  40 VNFRGEYGKTPLHlYLHYSSEKvkDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRT 119

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 30684671  119 PLHYAAQG--SHFEIVKYLVKKGASVRATTKAGKSPADV-----AGNAETQNFL 165
Cdd:PHA03095 120 PLHVYLSGfnINPKVIRLLLRKGADVNALDLYGMTPLAVllksrNANVELLRLL 173
Ank_4 pfam13637
Ankyrin repeats (many copies);
51-103 1.27e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.66  E-value: 1.27e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 30684671    51 RTPLHLAAWAGHNEVVSYLCKNKADVGAAAGDDMGAIHFASQKGHLEVVRTLL 103
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 19-149 1.79e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 57.31  E-value: 1.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684671   19 DLHSAARSGDLAAVQSIISSNPLAVNSRDKHSRTPLHLAAWAGHNEVVSYLCKNKADVGAAAGDDMGAIHFASQKGHLEV 98
Cdd:PHA02875  71 ELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKG 150

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 30684671   99 VRTLLSAGGSVKSITRKGLTPLHYAAQGSHFEIVKYLVKKGASVRATTKAG 149
Cdd:PHA02875 151 IELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNG 201
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 43-152 1.99e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 57.38  E-value: 1.99e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684671   43 VNSRDKHSRTPLHLAAWAGHNEVVSYLCKNKADVGAAAGDDMGAIHFASQKGHLEVVRT--------------------- 101
Cdd:PHA02876 171 VNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAiidnrsninkndlsllkairn 250

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684671  102 --------LLSAGGSVKSITRKGLTPLHYAAQG-SHFEIVKYLVKKGASVRATTKAGKSP 152
Cdd:PHA02876 251 edletsllLYDAGFSVNSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIKGETP 310
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 20-156 4.12e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 56.23  E-value: 4.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684671   20 LHSAARSG-DLAAVQSIISSNPlAVNSRDKHSRTPLHLAAWAGHN-EVVSYLCKNKADVGAAAGDDMGAIHFASQKGHLE 97
Cdd:PHA02876 311 LYLMAKNGyDTENIRTLIMLGA-DVNAADRLYITPLHQASTLDRNkDIVITLLELGANVNARDYCDKTPIHYAAVRNNVV 389

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684671   98 VVRTLLSAGGSVKSITRKGLTPLHYAAQGSH-FEIVKYLVKKGASVRATTKAGKSPADVA 156
Cdd:PHA02876 390 IINTLLDYGADIEALSQKIGTALHFALCGTNpYMSVKTLIDRGANVNSKNKDLSTPLHYA 449
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
35-178 9.25e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 54.57  E-value: 9.25e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684671  35 IISSNPLAVNSRDKHSRTPLHLAAWAGHNEVVSYLCKNKADVGAAAGDDMGAIHFASQKGHLEVVRTLLSAGGSVKSITR 114
Cdd:COG0666   6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30684671 115 KGLTPLHYAAQGSHFEIVKYLVKKGASVRATTKAGKSPADVA---GNAETQNFLEEceeqaRKAKVN 178
Cdd:COG0666  86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAaynGNLEIVKLLLE-----AGADVN 147
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 20-152 9.83e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 54.97  E-value: 9.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684671   20 LHSAARSGDLAAVQSIISSNPlAVNSRDKHSRTPLHLAAWAGHNEVVSYLCKNKADVGAAAGDDMGA------------- 86
Cdd:PHA02874  39 LIDAIRSGDAKIVELFIKHGA-DINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSILPIPCIEKdmiktildcgidv 117

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30684671   87 ----------IHFASQKGHLEVVRTLLSAGGSVKSITRKGLTPLHYAAQGSHFEIVKYLVKKGASVRATTKAGKSP 152
Cdd:PHA02874 118 nikdaelktfLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESP 193
PHA03095 PHA03095
ankyrin-like protein; Provisional
 64-152 1.02e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 55.03  E-value: 1.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684671   64 EVVSYLCKNKADVGAAAGDDMGAIHFASQKGH---LEVVRTLLSAGGSVKSITRKGLTPLH-YAAQGSHFEIVKYLVKKG 139
Cdd:PHA03095  28 EEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAG 107

                         90
                 ....*....|...
gi 30684671  140 ASVRATTKAGKSP 152
Cdd:PHA03095 108 ADVNAKDKVGRTP 120
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 43-156 1.10e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 55.07  E-value: 1.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684671   43 VNSRDKHSRTPLHLAAWAGHNEVVSYLCKNKADVGAAAGDDMGAIHFA-SQKGHLEVVRTLLSAGGSVKSITRKGLTPLH 121
Cdd:PHA02876 368 VNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLH 447

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 30684671  122 YAAQGS-HFEIVKYLVKKGASVRATTKAGKSPADVA 156
Cdd:PHA02876 448 YACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIA 483
PHA03095 PHA03095
ankyrin-like protein; Provisional
 43-156 2.40e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 53.88  E-value: 2.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684671   43 VNSRDKHSRTPLHlAAWAGHN---EVVSYLCKNKADVGAAAGDDMGA--IHFASQKGHLEVVRTLLSAGGSVKSITRKGL 117
Cdd:PHA03095 145 VNALDLYGMTPLA-VLLKSRNanvELLRLLIDAGADVYAVDDRFRSLlhHHLQSFKPRARIVRELIRAGCDPAATDMLGN 223

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 30684671  118 TPLHYAAQGSHFE--IVKYLVKKGASVRATTKAGKSPADVA 156
Cdd:PHA03095 224 TPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPLHYA 264
Ank_2 pfam12796
Ankyrin repeats (3 copies);
20-78 3.97e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 49.73  E-value: 3.97e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 30684671    20 LHSAARSGDLAAVQSIISSNplAVNSRDKHsRTPLHLAAWAGHNEVVSYLCKNKADVGA 78
Cdd:pfam12796  34 LHLAAKNGHLEIVKLLLEHA--DVNLKDNG-RTALHYAARSGHLEIVKLLLEKGADINV 89
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 23-144 5.08e-08

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: 53.09  E-value: 5.08e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684671  23 AARSGDLAAVQSIISSNPLAVNSRDKHSRTPLHLAAWAGHNEVVSYLCKNKAD-VGAAAGDDM----GAIHFASQKGHLE 97
Cdd:cd22192  24 AAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPMTSDLyqgeTALHIAVVNQNLN 103

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30684671  98 VVRTLLSAGGSVKS---------ITRKGLT-----PLHYAAQGSHFEIVKYLVKKGASVRA 144
Cdd:cd22192 104 LVRELIARGADVVSpratgtffrPGPKNLIyygehPLSFAACVGNEEIVRLLIEHGADIRA 164
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 43-142 6.41e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 52.36  E-value: 6.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684671   43 VNSRDKHSRTPLHLAAWAGHN--EVVSYLCKNKADVGAA--------------AGDDMG--AIHFASQKGHLEVVRTLLS 104
Cdd:PHA03100 134 VNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKnrvnyllsygvpinIKDVYGftPLHYAVYNNNPEFVKYLLD 213

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 30684671  105 AGGSVKSITRKGLTPLHYAAQGSHFEIVKYLVKKGASV 142
Cdd:PHA03100 214 LGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSI 251
Ank_4 pfam13637
Ankyrin repeats (many copies);
20-69 1.68e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.88  E-value: 1.68e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 30684671    20 LHSAARSGDLAAVQSIISsNPLAVNSRDKHSRTPLHLAAWAGHNEVVSYL 69
Cdd:pfam13637   5 LHAAAASGHLELLRLLLE-KGADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank_5 pfam13857
Ankyrin repeats (many copies);
102-156 2.03e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.57  E-value: 2.03e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 30684671   102 LLSAGG-SVKSITRKGLTPLHYAAQGSHFEIVKYLVKKGASVRATTKAGKSPADVA 156
Cdd:pfam13857   1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 47-142 2.45e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 51.02  E-value: 2.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684671   47 DKHSRTPLHLAAWAGHNEVVSYLCKNKADV-------GAAAGDDMGAIH------------------------FASQKGH 95
Cdd:PLN03192 555 DSKGRTPLHIAASKGYEDCVLVLLKHACNVhirdangNTALWNAISAKHhkifrilyhfasisdphaagdllcTAAKRND 634

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 30684671   96 LEVVRTLLSAGGSVKSITRKGLTPLHYAAQGSHFEIVKYLVKKGASV 142
Cdd:PLN03192 635 LTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 78-166 4.83e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.28  E-value: 4.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684671   78 AAAGDDMGAihfasqkghlevvRTLLSAGGSVKSITRKGLTPLHYAAQGSHFEIVKYLVKKGASVRATTKAGKSPADVAG 157
Cdd:PTZ00322  90 AASGDAVGA-------------RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAE 156


                 ....*....
gi 30684671  158 NAETQNFLE 166
Cdd:PTZ00322 157 ENGFREVVQ 165
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
20-120 5.38e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 49.57  E-value: 5.38e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684671  20 LHSAARSGDLAAVQSIISSNPlAVNSRDKHSRTPLHLAAWAGHNEVVSYLCKNKADVGAAAGDDMGAIHFASQKGHLEVV 99
Cdd:COG0666 190 LHLAAENGHLEIVKLLLEAGA-DVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIV 268

                        90       100
                ....*....|....*....|.
gi 30684671 100 RTLLSAGGSVKSITRKGLTPL 120
Cdd:COG0666 269 KLLLLALLLLAAALLDLLTLL 289
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 19-179 5.73e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 49.58  E-value: 5.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684671   19 DLHSAARSGDLAAVQSIISSNPLAVNSRDKHSRTPLHLAAWAGHNEVVSYLCKNKADVGAAAGDD----MGAIHFASQK- 93
Cdd:PHA02874   4 DLRMCIYSGDIEAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIphplLTAIKIGAHDi 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684671   94 ------------------GHLEVVRTLLSAGGSVKSITRKGLTPLHYAAQGSHFEIVKYLVKKGASVRATTKAGKSPADV 155
Cdd:PHA02874  84 ikllidngvdtsilpipcIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHI 163

                        170       180
                 ....*....|....*....|....
gi 30684671  156 AGNAETQNFLEECEEQARKAKVNN 179
Cdd:PHA02874 164 AIKHNFFDIIKLLLEKGAYANVKD 187
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 24-104 8.45e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.51  E-value: 8.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684671   24 ARSGDLAAVQSIISSNPlAVNSRDKHSRTPLHLAAWAGHNEVVSYLCKNKADVGAAAGDDMGAIHFASQKGHLEVVRTLL 103
Cdd:PTZ00322  90 AASGDAVGARILLTGGA-DPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168


                 .
gi 30684671  104 S 104
Cdd:PTZ00322 169 R 169
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 41-157 1.24e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.91  E-value: 1.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684671   41 LAVNSRDKHSRTPLHLAAWAGH-NEVVSYLCKNKADVGAAAGDDMGAIHFASQKGH-LEVVRTLLSAGGSVKSITRKGLT 118
Cdd:PHA02876 264 FSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYIT 343

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 30684671  119 PLHYAAQGSHF-EIVKYLVKKGASVRATTKAGKSPADVAG 157
Cdd:PHA02876 344 PLHQASTLDRNkDIVITLLELGANVNARDYCDKTPIHYAA 383
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 20-147 1.27e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.91  E-value: 1.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684671   20 LHSAARSGDLAAVQSIISSNPLAVNSRDKHSRTPLHLAAWAGHN-EVVSYLCKNKADVGAAAGDDMGAIHFASQ-KGHLE 97
Cdd:PHA02876 277 LHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYDtENIRTLIMLGADVNAADRLYITPLHQASTlDRNKD 356

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 30684671   98 VVRTLLSAGGSVKSITRKGLTPLHYAAQGSHFEIVKYLVKKGASVRATTK 147
Cdd:PHA02876 357 IVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQ 406
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 115-147 2.40e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 43.05  E-value: 2.40e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 30684671   115 KGLTPLHYAA-QGSHFEIVKYLVKKGASVRATTK 147
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 43-193 3.14e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 47.57  E-value: 3.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684671   43 VNSRDKHS-RTPLHLAAWAGHNEVVSYLCKNKADVGAAAGDDMGAIHFASQKGHLEVVRTLLSAGGSVKSITRKGLTPLH 121
Cdd:PHA02878 160 INMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLH 239

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30684671  122 YAAqGS--HFEIVKYLVKKGASVRA-TTKAGKSPADVAGNAETQ-NFLeeCEEQARKAKVNNEKKTEI---VKPESCSN 193
Cdd:PHA02878 240 ISV-GYckDYDILKLLLEHGVDVNAkSYILGLTALHSSIKSERKlKLL--LEYGADINSLNSYKLTPLssaVKQYLCIN 315
Ank_5 pfam13857
Ankyrin repeats (many copies);
40-90 8.84e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 8.84e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 30684671    40 PLAVNSRDKHSRTPLHLAAWAGHNEVVSYLCKNKADVGAAAGDDMGAIHFA 90
Cdd:pfam13857   6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 20-123 1.44e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 45.34  E-value: 1.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684671   20 LHSAARSGDLAAVQSIISSNPlAVNSRDKHSRTPLHLAAWAGHNEVVSYLCKNKADVGAAAGDDMGAIHFASQKGHLEVV 99
Cdd:PHA02874 128 LHYAIKKGDLESIKMLFEYGA-DVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACI 206

                         90       100
                 ....*....|....*....|....
gi 30684671  100 RTLLSAGGSVKSITRKGLTPLHYA 123
Cdd:PHA02874 207 KLLIDHGNHIMNKCKNGFTPLHNA 230
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 115-142 1.47e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 40.65  E-value: 1.47e-05
                           10        20
                   ....*....|....*....|....*...
gi 30684671    115 KGLTPLHYAAQGSHFEIVKYLVKKGASV 142
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
Ank_4 pfam13637
Ankyrin repeats (many copies);
116-156 2.17e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.11  E-value: 2.17e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 30684671   116 GLTPLHYAAQGSHFEIVKYLVKKGASVRATTKAGKSPADVA 156
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFA 41
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 64-156 2.96e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 44.49  E-value: 2.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684671   64 EVVSYLCKNKADVGAAAGD-DMGAIHFASQKGHLEVVRTLLSAGGSVKSITRKGLTPLHYAAQGSHFEIVKYLVKKGASV 142
Cdd:PHA02878 148 EITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAST 227

                         90
                 ....*....|....
gi 30684671  143 RATTKAGKSPADVA 156
Cdd:PHA02878 228 DARDKCGNTPLHIS 241
Ank_5 pfam13857
Ankyrin repeats (many copies);
86-123 3.58e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.41  E-value: 3.58e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 30684671    86 AIHFASQKGHLEVVRTLLSAGGSVKSITRKGLTPLHYA 123
Cdd:pfam13857  19 PLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 115-144 4.05e-05

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.55  E-value: 4.05e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 30684671   115 KGLTPLHYAAQGSHFEIVKYLVKKGASVRA 144
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 49-76 9.20e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.72  E-value: 9.20e-05
                           10        20
                   ....*....|....*....|....*...
gi 30684671     49 HSRTPLHLAAWAGHNEVVSYLCKNKADV 76
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 65-142 1.84e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 42.36  E-value: 1.84e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30684671   65 VVSYLCKNKADVGAAAGDDMGAIHFASQKGHLEVVRTLLSAGGSVKSITRKGLTPLHYAAQGSHFEIVKYLVKKGASV 142
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNI 237
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 20-83 2.22e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 42.16  E-value: 2.22e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30684671   20 LHSAARSGDLAAVQSIISSNpLAVNSRDKHSRTPLHLAAWAGHNEVVSYLCKNKADVGAAAGDD 83
Cdd:PLN03192 626 LCTAAKRNDLTAMKELLKQG-LNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDD 688
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 51-78 2.36e-04

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: 37.65  E-value: 2.36e-04
                          10        20
                  ....*....|....*....|....*....
gi 30684671    51 RTPLHLAAW-AGHNEVVSYLCKNKADVGA 78
Cdd:pfam00023   3 NTPLHLAAGrRGNLEIVKLLLSKGADVNA 31
PHA02798 PHA02798
ankyrin-like protein; Provisional
 32-151 5.98e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 40.59  E-value: 5.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684671   32 VQSIISSNPLAVNSRDKHSRTPLHLA---AWAGHNEVVSYLCKNKADVGAAAGDDMGAIHFASQKGH---LEVVRTLLSA 105
Cdd:PHA02798  91 IVKILIENGADINKKNSDGETPLYCLlsnGYINNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEK 170

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 30684671  106 GGSVKSITRK-GLTPLH----YAAQGSHFEIVKYLVKKGASVRATTKAGKS 151
Cdd:PHA02798 171 GVDINTHNNKeKYDTLHcyfkYNIDRIDADILKLFVDNGFIINKENKSHKK 221
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 20-176 6.39e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 40.33  E-value: 6.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684671   20 LHSAARSGDLAAVQSIISsNPLAVNSRDKHSRTPLHLAAWagHNEVVSYLCKNKADVGAAAGDDMGAIHFASQ-KGHLEV 98
Cdd:PHA02874 194 LHNAAEYGDYACIKLLID-HGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAINpPCDIDI 270

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684671   99 VRTLLSAGGSVKSITRKGLTPLHYAAQG-SHFEIVKYLVkkgASVRATTKAGKSPA-------DVAGNAETQNFLEECEE 170
Cdd:PHA02874 271 IDILLYHKADISIKDNKGENPIDTAFKYiNKDPVIKDII---ANAVLIKEADKLKDsdflehiEIKDNKEFSDFIKECNE 347


                 ....*.
gi 30684671  171 QARKAK 176
Cdd:PHA02874 348 EIEDMK 353
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 22-145 9.41e-04

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 40.06  E-value: 9.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684671    22 SAARSGDLAAVQSII-SSNPLAVNSRDKHSRTPLHLAAWAGHN-EVVSYLCKNKADVgaAAGDdmGAIHFASqKGHLEVV 99
Cdd:TIGR00870  23 PAAERGDLASVYRDLeEPKKLNINCPDRLGRSALFVAAIENENlELTELLLNLSCRG--AVGD--TLLHAIS-LEYVDAV 97

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684671   100 RTLLS-----AGGSV---------KSITRKGLTPLHYAAQGSHFEIVKYLVKKGASVRAT 145
Cdd:TIGR00870  98 EAILLhllaaFRKSGplelandqyTSEFTPGITALHLAAHRQNYEIVKLLLERGASVPAR 157
PHA03095 PHA03095
ankyrin-like protein; Provisional
 20-144 1.67e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 39.24  E-value: 1.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684671   20 LHSAARSGDLAA--VQSIISSNpLAVNSRDKHSRTPLHLAAWAGHNEVVSYLCKNKADVGAAAGDDMGAIHFASQKGHLE 97
Cdd:PHA03095 226 LHSMATGSSCKRslVLPLLIAG-ISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGR 304

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 30684671   98 VVRTLLSAGGSVKSITRKgltpLHYAAQGSHF-------EIVKYLV-KKGASVRA 144
Cdd:PHA03095 305 AVRAALAKNPSAETVAAT----LNTASVAGGDipsdatrLCVAKVVlRGAFSLLP 355
 
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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