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Conserved domains on  [gi|194018403|ref|NP_001123453|]
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ankyrin repeat domain-containing protein 2 isoform b [Homo sapiens]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 11429852)

ankyrin repeat domain-containing protein; ANK proteins mediate specific protein-protein interactions without necessarily recognizing specific primary sequences which allows for one ankyrin repeat domain to recognize and bind to a variety of intracellular substrates and may be involved in a wide array of functions

Gene Ontology:  GO:0005515
PubMed:  17176038
SCOP:  4000366

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
70-286 4.64e-33

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 123.91  E-value: 4.64e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018403  70 LLVLEDEKHHGAQSAALQKVKGQERVRKTSLDLRREIIDVGGIQNLIELRKKRKQKKRDALAASHEPPPEPEEITGPVDE 149
Cdd:COG0666    9 LLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGN 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018403 150 ETFLKAAVEGKMKVIEKFLADGGSADTCDQFRRTALHRASLEGHMEILEKLLDNGATVDFQDRLDCTAMHWACRGGHLEV 229
Cdd:COG0666   89 TLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEI 168

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 194018403 230 VKLLQSHGADTNVRDKEGDTALHDAVRLNRYKIIKLLLLHGADMMTKNLAGKTPTDL 286
Cdd:COG0666  169 VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDL 225
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
70-286 4.64e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 123.91  E-value: 4.64e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018403  70 LLVLEDEKHHGAQSAALQKVKGQERVRKTSLDLRREIIDVGGIQNLIELRKKRKQKKRDALAASHEPPPEPEEITGPVDE 149
Cdd:COG0666    9 LLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGN 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018403 150 ETFLKAAVEGKMKVIEKFLADGGSADTCDQFRRTALHRASLEGHMEILEKLLDNGATVDFQDRLDCTAMHWACRGGHLEV 229
Cdd:COG0666   89 TLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEI 168

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 194018403 230 VKLLQSHGADTNVRDKEGDTALHDAVRLNRYKIIKLLLLHGADMMTKNLAGKTPTDL 286
Cdd:COG0666  169 VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDL 225
Ank_2 pfam12796
Ankyrin repeats (3 copies);
185-277 6.92e-24

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 93.26  E-value: 6.92e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018403  185 LHRASLEGHMEILEKLLDNGATVDFQDRLDCTAMHWACRGGHLEVVKLLQSHgADTNVRDkEGDTALHDAVRLNRYKIIK 264
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 194018403  265 LLLLHGADMMTKN 277
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 160-285 5.87e-18

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 84.31  E-value: 5.87e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018403 160 KMKVIEKFLADGGSADTCDQFRRTALH---RASLEGHMEILEKLLDNGATVDFQDRLDCTAMH-WACRGGHLEVVKLLQS 235
Cdd:PHA03095  26 TVEEVRRLLAAGADVNFRGEYGKTPLHlylHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIK 105

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 194018403 236 HGADTNVRDKEGDTALHdaVRLN----RYKIIKLLLLHGADMMTKNLAGKTPTD 285
Cdd:PHA03095 106 AGADVNAKDKVGRTPLH--VYLSgfniNPKVIRLLLRKGADVNALDLYGMTPLA 157
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 153-283 5.31e-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: 48.09  E-value: 5.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018403 153 LKAAVEGKMKVIEKFLadggSADTCDQFRR-----TALHRASLEGHMEILEKLLDNG-------ATVDFQdrLDCTAMHW 220
Cdd:cd22192   22 LLAAKENDVQAIKKLL----KCPSCDLFQRgalgeTALHVAALYDNLEAAVVLMEAApelvnepMTSDLY--QGETALHI 95

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 194018403 221 ACRGGHLEVVKLLQSHGADTN---------VRDKE-----GDTALHDAVRLNRYKIIKLLLLHGADMMTKNLAGKTP 283
Cdd:cd22192   96 AVVNQNLNLVRELIARGADVVspratgtffRPGPKnliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTV 172
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 214-242 5.69e-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: 42.57  E-value: 5.69e-06
                           10        20
                   ....*....|....*....|....*....
gi 194018403   214 DCTAMHWACRGGHLEVVKLLQSHGADTNV 242
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 149-272 5.89e-05

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: 44.69  E-value: 5.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018403  149 EETFLKAAVEGKMKVIEKFLADGGSA--DTCDQFRRTALHRASLEG----HMEILEKLLDNGATVDfqdrldcTAMHwAC 222
Cdd:TIGR00870  18 EKAFLPAAERGDLASVYRDLEEPKKLniNCPDRLGRSALFVAAIENenleLTELLLNLSCRGAVGD-------TLLH-AI 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194018403  223 RGGHLEVVK-----LLQSHGADTN---VRDKEGD------TALHDAVRLNRYKIIKLLLLHGAD 272
Cdd:TIGR00870  90 SLEYVDAVEaillhLLAAFRKSGPlelANDQYTSeftpgiTALHLAAHRQNYEIVKLLLERGAS 153
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
70-286 4.64e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 123.91  E-value: 4.64e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018403  70 LLVLEDEKHHGAQSAALQKVKGQERVRKTSLDLRREIIDVGGIQNLIELRKKRKQKKRDALAASHEPPPEPEEITGPVDE 149
Cdd:COG0666    9 LLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGN 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018403 150 ETFLKAAVEGKMKVIEKFLADGGSADTCDQFRRTALHRASLEGHMEILEKLLDNGATVDFQDRLDCTAMHWACRGGHLEV 229
Cdd:COG0666   89 TLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEI 168

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 194018403 230 VKLLQSHGADTNVRDKEGDTALHDAVRLNRYKIIKLLLLHGADMMTKNLAGKTPTDL 286
Cdd:COG0666  169 VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDL 225
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
100-283 2.21e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 113.90  E-value: 2.21e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018403 100 LDLRREIIDVGGIQNLIELRKKRKQKKRDALAASHEPPPEPEEITGPVDEETFLKAAVEGKMKVIEKFLADGGSADTCDQ 179
Cdd:COG0666    6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018403 180 FRRTALHRASLEGHMEILEKLLDNGATVDFQDRLDCTAMHWACRGGHLEVVKLLQSHGADTNVRDKEGDTALHDAVRLNR 259
Cdd:COG0666   86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165

                        170       180
                 ....*....|....*....|....
gi 194018403 260 YKIIKLLLLHGADMMTKNLAGKTP 283
Cdd:COG0666  166 LEIVKLLLEAGADVNARDNDGETP 189
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
155-286 6.52e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 112.74  E-value: 6.52e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018403 155 AAVEGKMKVIEKFLADGGSADTCDQFRRTALHRASLEGHMEILEKLLDNGATVDFQDRLDCTAMHWACRGGHLEVVKLLQ 234
Cdd:COG0666  127 AAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLL 206

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 194018403 235 SHGADTNVRDKEGDTALHDAVRLNRYKIIKLLLLHGADMMTKNLAGKTPTDL 286
Cdd:COG0666  207 EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLL 258
Ank_2 pfam12796
Ankyrin repeats (3 copies);
185-277 6.92e-24

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 93.26  E-value: 6.92e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018403  185 LHRASLEGHMEILEKLLDNGATVDFQDRLDCTAMHWACRGGHLEVVKLLQSHgADTNVRDkEGDTALHDAVRLNRYKIIK 264
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 194018403  265 LLLLHGADMMTKN 277
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 160-285 5.87e-18

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 84.31  E-value: 5.87e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018403 160 KMKVIEKFLADGGSADTCDQFRRTALH---RASLEGHMEILEKLLDNGATVDFQDRLDCTAMH-WACRGGHLEVVKLLQS 235
Cdd:PHA03095  26 TVEEVRRLLAAGADVNFRGEYGKTPLHlylHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIK 105

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 194018403 236 HGADTNVRDKEGDTALHdaVRLN----RYKIIKLLLLHGADMMTKNLAGKTPTD 285
Cdd:PHA03095 106 AGADVNAKDKVGRTPLH--VYLSgfniNPKVIRLLLRKGADVNALDLYGMTPLA 157
Ank_2 pfam12796
Ankyrin repeats (3 copies);
155-244 2.19e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.92  E-value: 2.19e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018403  155 AAVEGKMKVIEKFLADGGSADTCDQFRRTALHRASLEGHMEILEKLLDNgATVDFQDRlDCTAMHWACRGGHLEVVKLLQ 234
Cdd:pfam12796   4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLL 81

                          90
                  ....*....|
gi 194018403  235 SHGADTNVRD 244
Cdd:pfam12796  82 EKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
155-282 2.30e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 80.77  E-value: 2.30e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018403 155 AAVEGKMKVIEKFLADGGSADTCDQFRRTALHRASLEGHMEILEKLLDNGATVDFQDRLDCTAMHWACRGGHLEVVKLLQ 234
Cdd:COG0666  160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 194018403 235 SHGADTNVRDKEGDTALHDAVRLNRYKIIKLLLLHGADMMTKNLAGKT 282
Cdd:COG0666  240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 163-283 1.20e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 77.31  E-value: 1.20e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018403 163 VIEKFLADGGSADTCDQFRRTALHRASLEGHMEILEKLLDNGATVDFQDRLDCTAMHWACRGGHLEVVKLLQSHGADTNV 242
Cdd:PHA02874 106 MIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANV 185

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 194018403 243 RDKEGDTALHDAVRLNRYKIIKLLLLHGADMMTKNLAGKTP 283
Cdd:PHA02874 186 KDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTP 226
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 195-283 2.45e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 73.07  E-value: 2.45e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018403 195 EILEKLLDNGATVDFQDRLDCTAMHWACRGGHLEVVKLLQSHGADTNVRDKEGDTALHDAVRLNRYKIIKLLLLHGADMM 274
Cdd:PHA02874 105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184


                 ....*....
gi 194018403 275 TKNLAGKTP 283
Cdd:PHA02874 185 VKDNNGESP 193
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 162-321 1.55e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 71.06  E-value: 1.55e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018403 162 KVIEKFLADGGSADTCDQFR-RTALHRASLEGHMEILEKLLDNGATVDFQDRLDCTAMHWACRGGHLEVVKLLQSHGADT 240
Cdd:PHA02878 148 EITKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAST 227

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018403 241 NVRDKEGDTALHDAV-RLNRYKIIKLLLLHGADMMTKN-LAGKTPTDLVQLWQADTRHALEHpepGAEHNGLegpnDSGR 318
Cdd:PHA02878 228 DARDKCGNTPLHISVgYCKDYDILKLLLEHGVDVNAKSyILGLTALHSSIKSERKLKLLLEY---GADINSL----NSYK 300


                 ...
gi 194018403 319 ETP 321
Cdd:PHA02878 301 LTP 303
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 160-277 2.05e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 70.46  E-value: 2.05e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018403 160 KMKVIEKFLADGGSADTCDQFRRTALHRASLEGH-----MEILEKLLDNGATVDFQDRLDCTAMHWA--CRGGHLEVVKL 232
Cdd:PHA03100  47 NIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITPLLYAisKKSNSYSIVEY 126

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 194018403 233 LQSHGADTNVRDKEGDTALHDAVRLNRY--KIIKLLLLHGADMMTKN 277
Cdd:PHA03100 127 LLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKN 173
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 159-272 4.53e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 69.31  E-value: 4.53e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018403 159 GKMKVIEKFLADGGSADTCDQFRRTALHrASLEG---HMEILEKLLDNGATVDFQDRLDC----------------TAMH 219
Cdd:PHA03100 119 NSYSIVEYLLDNGANVNIKNSDGENLLH-LYLESnkiDLKILKLLIDKGVDINAKNRVNYllsygvpinikdvygfTPLH 197

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 194018403 220 WACRGGHLEVVKLLQSHGADTNVRDKEGDTALHDAVRLNRYKIIKLLLLHGAD 272
Cdd:PHA03100 198 YAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
Ank_4 pfam13637
Ankyrin repeats (many copies);
181-233 1.44e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.83  E-value: 1.44e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 194018403  181 RRTALHRASLEGHMEILEKLLDNGATVDFQDRLDCTAMHWACRGGHLEVVKLL 233
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 155-272 3.23e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 63.86  E-value: 3.23e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018403 155 AAVEGKMKVIEKFLADGGSADTCDQFRRTALHRASLEGHMEILEKLLDNGATVDFQDRLDCTAMHWACRGGHLEVVKLLQ 234
Cdd:PHA02875 109 ATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLL 188

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 194018403 235 SHGADTNVRDKEGD-TALHDAVRLNRYKIIKLLLLHGAD 272
Cdd:PHA02875 189 DSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGAD 227
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 194-283 6.64e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 62.76  E-value: 6.64e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018403 194 MEILEKLLDNGATVDFQDRLDCTAMHWACRGGH-----LEVVKLLQSHGADTNVRDKEGDTALHDAV--RLNRYKIIKLL 266
Cdd:PHA03100  48 IDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYL 127

                         90
                 ....*....|....*..
gi 194018403 267 LLHGADMMTKNLAGKTP 283
Cdd:PHA03100 128 LDNGANVNIKNSDGENL 144
Ank_4 pfam13637
Ankyrin repeats (many copies);
216-267 1.76e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.74  E-value: 1.76e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 194018403  216 TAMHWACRGGHLEVVKLLQSHGADTNVRDKEGDTALHDAVRLNRYKIIKLLL 267
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 162-287 1.51e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 58.74  E-value: 1.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018403 162 KVIEKFLADGGSADTCDQFRRTALHRASLEGHMEILEKLLDNGATVDFQDRLDCTAMHWAC-RGGHLEVVKLLQSHGADT 240
Cdd:PHA02878 182 RLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVgYCKDYDILKLLLEHGVDV 261

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 194018403 241 NVRDK-EGDTALHDAVRLNRykIIKLLLLHGADMMTKNLAGKTPTDLV 287
Cdd:PHA02878 262 NAKSYiLGLTALHSSIKSER--KLKLLLEYGADINSLNSYKLTPLSSA 307
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 152-266 1.72e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 59.11  E-value: 1.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018403 152 FLKAAVEGKMKVIEKFLADGGSADTCDQFRRTALHRASLeGHMEILEKLLDNGATVDFQDRLDCTAMHWACRGGHLEVVK 231
Cdd:PLN03192 497 FLQHHKELHDLNVGDLLGDNGGEHDDPNMASNLLTVAST-GNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVL 575

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 194018403 232 LLQSHGADTNVRDKEGDTALHDAVRLNRYKIIKLL 266
Cdd:PLN03192 576 VLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 150-301 2.29e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 58.05  E-value: 2.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018403 150 ETFLKAAVE-GKMKVIEKFLADGGSADTCDQFRRTALHRASLEGHMEILEKLLDNGATVDFQDRLDCTAMHWACRGGHLE 228
Cdd:PHA02874 125 KTFLHYAIKkGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYA 204

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 194018403 229 VVKLLQSHGADTNVRDKEGDTALHDAVRLNRYKIikLLLLHGADMMTKNLAGKTPtdlvqlwqadTRHALEHP 301
Cdd:PHA02874 205 CIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAI--ELLINNASINDQDIDGSTP----------LHHAINPP 265
PHA03095 PHA03095
ankyrin-like protein; Provisional
 162-283 2.51e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 58.11  E-value: 2.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018403 162 KVIEKFLADGGSADTCDQFRRTALHR--ASLEGHMEILEKLLDNGATVDFQDRLDCTAMHWACR--GGHLEVVKLLQSHG 237
Cdd:PHA03095  98 DVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKsrNANVELLRLLIDAG 177

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 194018403 238 ADTNVRDKEGDTALH---DAVRlNRYKIIKLLLLHGADMMTKNLAGKTP 283
Cdd:PHA03095 178 ADVYAVDDRFRSLLHhhlQSFK-PRARIVRELIRAGCDPAATDMLGNTP 225
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 144-291 3.40e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 57.96  E-value: 3.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018403 144 TGPVDEETFLKAAVEGKMKVIEKFLADGGSADTCDQFRRTALHRASLEGHMEILEKLLDNGATVDFQDRLDCTAMhW--- 220
Cdd:PLN03192 521 DDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTAL-Wnai 599

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018403 221 -----------------------------ACRGGHLEVVKLLQSHGADTNVRDKEGDTALHDAVRLNRYKIIKLLLLHGA 271
Cdd:PLN03192 600 sakhhkifrilyhfasisdphaagdllctAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGA 679

                        170       180
                 ....*....|....*....|.
gi 194018403 272 DMMTKNLAGK-TPTDLVQLWQ 291
Cdd:PLN03192 680 DVDKANTDDDfSPTELRELLQ 700
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
161-283 6.75e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 56.12  E-value: 6.75e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018403 161 MKVIEKFLADGGSADTCDQFRRTALHRASLEGHMEILEKLLDNGATVDFQDRLDCTAMHWACRGGHLEVVKLLQSHGADT 240
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 194018403 241 NVRDKEGDTALHDAVRLNRYKIIKLLLLHGADMMTKNLAGKTP 283
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETP 123
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 155-283 1.02e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 56.15  E-value: 1.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018403 155 AAVEGKMKVIEKFLADGGSADtcDQFRR---TALHRASLEGHMEILEKLLDNGATVDFQDRLDCTAMHWACRGGHLEVVK 231
Cdd:PHA02875  75 AVEEGDVKAVEELLDLGKFAD--DVFYKdgmTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIE 152

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 194018403 232 LLQSHGADTNVRDKEGDTALHDAVRLNRYKIIKLLLLHGADMmtkNLAGKTP 283
Cdd:PHA02875 153 LLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANI---DYFGKNG 201
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 200-302 1.12e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.45  E-value: 1.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018403 200 LLDNGATVDFQDRLDCTAMHWACRGGHLEVVKLLQSHGADTNVRDKEGDTALHDAVRLNRYKIIKLLLLH-------GAD 272
Cdd:PTZ00322 101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHsqchfelGAN 180

                         90       100       110
                 ....*....|....*....|....*....|
gi 194018403 273 MMTKNLAGKTPTdlvqlwQADTRHALEHPE 302
Cdd:PTZ00322 181 AKPDSFTGKPPS------LEDSPISSHHPD 204
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 167-283 1.37e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 56.23  E-value: 1.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018403 167 FLADGG-SADTCDQFRRTALHRASLEGHM-EILEKLLDNGATVDFQDRLDCTAMHWACRGGH-LEVVKLLQSHGADTNVR 243
Cdd:PHA02876 258 LLYDAGfSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAA 337

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 194018403 244 DKEGDTALHDAVRLNRYKIIKLLLLH-GADMMTKNLAGKTP 283
Cdd:PHA02876 338 DRLYITPLHQASTLDRNKDIVITLLElGANVNARDYCDKTP 378
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 164-283 2.12e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 55.45  E-value: 2.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018403 164 IEKFLADGGSADTCDQFRRTALHRAS-LEGHMEILEKLLDNGATVDFQDRLDCTAMHWACRGGHLEVVKLLQSHGADTNV 242
Cdd:PHA02876 324 IRTLIMLGADVNAADRLYITPLHQAStLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEA 403

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 194018403 243 RDKEGDTALHDAV-RLNRYKIIKLLLLHGADMMTKNLAGKTP 283
Cdd:PHA02876 404 LSQKIGTALHFALcGTNPYMSVKTLIDRGANVNSKNKDLSTP 445
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 180-305 2.69e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 55.29  E-value: 2.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018403 180 FRRTALHR---ASLEGHMEILEKLLDNGATVDF----QDRLDCTAMHWA----CR---GGHLEVVKLLQSHGADTNVRDK 245
Cdd:PTZ00322  34 FERMAAIQeeiARIDTHLEALEATENKDATPDHnlttEEVIDPVVAHMLtvelCQlaaSGDAVGARILLTGGADPNCRDY 113

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194018403 246 EGDTALHDAVRLNRYKIIKLLLLHGADMMTKNLAGKTPTDLV------QLWQADTRHALEHPEPGA 305
Cdd:PTZ00322 114 DGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAeengfrEVVQLLSRHSQCHFELGA 179
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 155-285 4.37e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 51.22  E-value: 4.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018403 155 AAVEGKMKVIEKFLADGGSADTCDQFRRTALHRA--SLEGHMEIlEKLLDNGATVDFQDRLDCTAMHWACRGG-HLEVVK 231
Cdd:PHA02876 382 AAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlcGTNPYMSV-KTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIE 460

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 194018403 232 LLQSHGADTNVRDKEGDTALhdAVRLNRYKIIKLLLLHGADMMTKNLAGKTPTD 285
Cdd:PHA02876 461 MLLDNGADVNAINIQNQYPL--LIALEYHGIVNILLHYGAELRDSRVLHKSLND 512
Ank_5 pfam13857
Ankyrin repeats (many copies);
200-252 7.58e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.42  E-value: 7.58e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 194018403  200 LLDNG-ATVDFQDRLDCTAMHWACRGGHLEVVKLLQSHGADTNVRDKEGDTALH 252
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 162-267 4.93e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 47.71  E-value: 4.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018403 162 KVIEKFLADGGSADTCDQFRRTALHRASLEGHME--ILEKLLDNGATVDFQDRLDCTAMHWA-CRGGHLEVVKLLQShGA 238
Cdd:PHA03095 203 RIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPLHYAaVFNNPRACRRLIAL-GA 281

                         90       100
                 ....*....|....*....|....*....
gi 194018403 239 DTNVRDKEGDTALHDAVRLNRYKIIKLLL 267
Cdd:PHA03095 282 DINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 153-283 5.31e-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: 48.09  E-value: 5.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018403 153 LKAAVEGKMKVIEKFLadggSADTCDQFRR-----TALHRASLEGHMEILEKLLDNG-------ATVDFQdrLDCTAMHW 220
Cdd:cd22192   22 LLAAKENDVQAIKKLL----KCPSCDLFQRgalgeTALHVAALYDNLEAAVVLMEAApelvnepMTSDLY--QGETALHI 95

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 194018403 221 ACRGGHLEVVKLLQSHGADTN---------VRDKE-----GDTALHDAVRLNRYKIIKLLLLHGADMMTKNLAGKTP 283
Cdd:cd22192   96 AVVNQNLNLVRELIARGADVVspratgtffRPGPKnliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTV 172
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 214-242 5.69e-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: 42.57  E-value: 5.69e-06
                           10        20
                   ....*....|....*....|....*....
gi 194018403   214 DCTAMHWACRGGHLEVVKLLQSHGADTNV 242
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 182-291 6.92e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 47.29  E-value: 6.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018403 182 RTALHRASLEGHMEILEKLLDNGATVDFQDRLDCTAMHWACRGGHLEVVKLLQSHGADTNVRDKEGDTALHDAVRLNRYK 261
Cdd:PHA02875   3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82

                         90       100       110
                 ....*....|....*....|....*....|...
gi 194018403 262 IIKLLLLHGA---DMMTKNlaGKTPTDLVQLWQ 291
Cdd:PHA02875  83 AVEELLDLGKfadDVFYKD--GMTPLHLATILK 113
Ank_5 pfam13857
Ankyrin repeats (many copies);
232-287 7.93e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.72  E-value: 7.93e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 194018403  232 LLQSHGADTNVRDKEGDTALHDAVRLNRYKIIKLLLLHGADMMTKNLAGKTPTDLV 287
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 168-236 1.08e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.20  E-value: 1.08e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 194018403 168 LADGGSADTCDQFRRTALHRASLEGHMEILEKLLDNGATVDFQDRLDCTAMHWACRGGHLEVVKLLQSH 236
Cdd:PTZ00322 102 LTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 191-279 1.39e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.60  E-value: 1.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018403 191 EGHMEILEKLLDNGATVDFQDRLDCTAMHWACRGGHLEVVKLLQSHGADTNVRDKEGDTALHDAVRLNRYKIIKLLLLHG 270
Cdd:PHA02876 155 QDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNR 234


                 ....*....
gi 194018403 271 ADMMTKNLA 279
Cdd:PHA02876 235 SNINKNDLS 243
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 162-269 1.49e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 46.41  E-value: 1.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018403 162 KVIEKFLADGGSADTCDQFRRTALHRASleGHM---EILEKLLDNGATVDFQDR-LDCTAMHWACRGGhlEVVKLLQSHG 237
Cdd:PHA02878 215 PIVHILLENGASTDARDKCGNTPLHISV--GYCkdyDILKLLLEHGVDVNAKSYiLGLTALHSSIKSE--RKLKLLLEYG 290

                         90       100       110
                 ....*....|....*....|....*....|...
gi 194018403 238 ADTNVRDKEGDTALHDAVRLNR-YKIIKLLLLH 269
Cdd:PHA02878 291 ADINSLNSYKLTPLSSAVKQYLcINIGRILISN 323
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 215-245 1.50e-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. 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: 41.12  E-value: 1.50e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 194018403  215 CTAMHWAC-RGGHLEVVKLLQSHGADTNVRDK 245
Cdd:pfam00023   3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
155-251 3.55e-05

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 44.94  E-value: 3.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018403 155 AAVEGKMKVIEKFLADGGSADTCDQFRRTALHRASLEGHMEILEKLLDNGATVDFQDRLDCTAMHWACRGGHLEVVKLLQ 234
Cdd:COG0666  193 AAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLL 272

                         90
                 ....*....|....*..
gi 194018403 235 SHGADTNVRDKEGDTAL 251
Cdd:COG0666  273 LALLLLAAALLDLLTLL 289
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 148-242 4.41e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 44.98  E-value: 4.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018403 148 DEETFLKAAV-EGKMKVIEKFLADGGSADTCDQFRRTALHRASLEGHMEILEKLLDNGATVD-FQDRLDCTAMHWACRGG 225
Cdd:PHA02875 134 DKFSPLHLAVmMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDyFGKNGCVAALCYAIENN 213

                         90
                 ....*....|....*..
gi 194018403 226 HLEVVKLLQSHGADTNV 242
Cdd:PHA02875 214 KIDIVRLFIKRGADCNI 230
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 149-272 5.89e-05

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: 44.69  E-value: 5.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018403  149 EETFLKAAVEGKMKVIEKFLADGGSA--DTCDQFRRTALHRASLEG----HMEILEKLLDNGATVDfqdrldcTAMHwAC 222
Cdd:TIGR00870  18 EKAFLPAAERGDLASVYRDLEEPKKLniNCPDRLGRSALFVAAIENenleLTELLLNLSCRGAVGD-------TLLH-AI 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194018403  223 RGGHLEVVK-----LLQSHGADTN---VRDKEGD------TALHDAVRLNRYKIIKLLLLHGAD 272
Cdd:TIGR00870  90 SLEYVDAVEaillhLLAAFRKSGPlelANDQYTSeftpgiTALHLAAHRQNYEIVKLLLERGAS 153
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 158-287 1.39e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 43.51  E-value: 1.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018403 158 EGKMKVIEKFLADGGSADTCDQFRRTALHRASLEGHMEILEKLLDNGATVDFQDRLDCTAMHWACRGGHLEVVK------ 231
Cdd:PHA02876 155 QDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKaiidnr 234

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018403 232 -----------------------LLQSHGADTNVRDKEGDTALHDAVRL-NRYKIIKLLLLHGADMMTKNLAGKTPTDLV 287
Cdd:PHA02876 235 sninkndlsllkairnedletslLLYDAGFSVNSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIKGETPLYLM 314
Ank_4 pfam13637
Ankyrin repeats (many copies);
150-201 1.55e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.79  E-value: 1.55e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 194018403  150 ETFLKAAVEGKMKVIEKFLADGGSADTCDQFRRTALHRASLEGHMEILEKLL 201
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 150-283 2.01e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 42.64  E-value: 2.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018403 150 ETFLKAAVE-GKMKVIeKFLADGGS--ADTCDQfRRTALHRASLEGHMEIleKLLDNGATVDFQDRLDCTAMHWA----C 222
Cdd:PHA02874 191 ESPLHNAAEyGDYACI-KLLIDHGNhiMNKCKN-GFTPLHNAIIHNRSAI--ELLINNASINDQDIDGSTPLHHAinppC 266

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 194018403 223 rggHLEVVKLLQSHGADTNVRDKEGDTALHDAVR-LNRYKIIKLLLlhgADMMTKNLAGKTP 283
Cdd:PHA02874 267 ---DIDIIDILLYHKADISIKDNKGENPIDTAFKyINKDPVIKDII---ANAVLIKEADKLK 322
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 192-272 3.13e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 42.26  E-value: 3.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018403 192 GHMEILEKLLDN-GATVDFQDRLDCTAMHWACRGGHLEVVKLLQSHGADTNVRDKEGDTALHDAVRLNRYKIIKLLLLHG 270
Cdd:PHA02874  12 GDIEAIEKIIKNkGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG 91


                 ..
gi 194018403 271 AD 272
Cdd:PHA02874  92 VD 93
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 216-242 3.61e-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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.24  E-value: 3.61e-04
                          10        20
                  ....*....|....*....|....*..
gi 194018403  216 TAMHWACRGGHLEVVKLLQSHGADTNV 242
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADINA 30
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 228-283 6.14e-04

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 39.86  E-value: 6.14e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 194018403 228 EVVKLLQSHGADTNVRD-KEGDTALHDAVRLNRYKIIKLLLLH-GADMMTKNLAGKTP 283
Cdd:PHA02736  72 EKLKLLMEWGADINGKErVFGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTP 129
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 246-273 6.57e-04

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: 36.41  E-value: 6.57e-04
                           10        20
                   ....*....|....*....|....*...
gi 194018403   246 EGDTALHDAVRLNRYKIIKLLLLHGADM 273
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 182-208 7.69e-04

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: 36.41  E-value: 7.69e-04
                           10        20
                   ....*....|....*....|....*..
gi 194018403   182 RTALHRASLEGHMEILEKLLDNGATVD 208
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 195-283 8.13e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 40.80  E-value: 8.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018403 195 EILEKLLDNGATVDFQDRLDCTAMHWACRGGHLEVVKLLQSHGADTNVRDKEGDTALH-----DAVRLNRYKIIKLLLLH 269
Cdd:PHA03100  16 KNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEY 95

                         90
                 ....*....|....
gi 194018403 270 GADMMTKNLAGKTP 283
Cdd:PHA03100  96 GANVNAPDNNGITP 109
PHA02798 PHA02798
ankyrin-like protein; Provisional
 227-283 9.19e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 40.97  E-value: 9.19e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 194018403 227 LEVVKLLQSHGADTNVRDKEGDTALHDAV-RLNRYK----IIKLLLLHGADMMTKNLAGKTP 283
Cdd:PHA02798  51 TDIVKLFINLGANVNGLDNEYSTPLCTILsNIKDYKhmldIVKILIENGADINKKNSDGETP 112
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 194-283 1.07e-03

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 40.67  E-value: 1.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018403 194 MEILEKLLDNGATVDFQDRLDCTAMH-WACRGG-HLEVVKLLQSHGADTNVRDKEGDTALHDAV-RLN------------ 258
Cdd:PHA02716 297 ISVVYSFLQPGVKLHYKDSAGRTCLHqYILRHNiSTDIIKLLHEYGNDLNEPDNIGNTVLHTYLsMLSvvnildpetdnd 376

                         90       100
                 ....*....|....*....|....*.
gi 194018403 259 -RYKIIKLLLLHGADMMTKNLAGKTP 283
Cdd:PHA02716 377 iRLDVIQCLISLGADITAVNCLGYTP 402
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 246-277 1.53e-03

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: 35.73  E-value: 1.53e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 194018403  246 EGDTALHDAV-RLNRYKIIKLLLLHGADMMTKN 277
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA02917 PHA02917
ankyrin-like protein; Provisional
 218-282 2.10e-03

ankyrin-like protein; Provisional


Pssm-ID: 165231 [Multi-domain]  Cd Length: 661  Bit Score: 39.98  E-value: 2.10e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194018403 218 MHWACRggHLEVVKLLQSHGADTNVRDKEGDTALHDAVRLNRYKIIKLLLLHGADMMTKNLAGKT 282
Cdd:PHA02917 425 MSYACP--ILSTINICLPYLKDINMIDKRGETLLHKAVRYNKQSLVSLLLESGSDVNIRSNNGYT 487
PHA02798 PHA02798
ankyrin-like protein; Provisional
 185-272 2.38e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 39.43  E-value: 2.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018403 185 LHRASLEghMEILEKLLDNGATVDFQDRLD----CTAMHWACRGGH-LEVVKLLQSHGADTNVRDKEGDTA----LHDAV 255
Cdd:PHA02798  44 LQRDSPS--TDIVKLFINLGANVNGLDNEYstplCTILSNIKDYKHmLDIVKILIENGADINKKNSDGETPlyclLSNGY 121

                         90
                 ....*....|....*..
gi 194018403 256 rLNRYKIIKLLLLHGAD 272
Cdd:PHA02798 122 -INNLEILLFMIENGAD 137
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 246-272 3.23e-03

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: 34.54  E-value: 3.23e-03
                          10        20
                  ....*....|....*....|....*..
gi 194018403  246 EGDTALHDAVRLNRYKIIKLLLLHGAD 272
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGAD 27
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 182-212 4.38e-03

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: 34.19  E-value: 4.38e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 194018403  182 RTALHRASLE-GHMEILEKLLDNGATVDFQDR 212
Cdd:pfam00023   3 NTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 146-275 4.61e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 38.91  E-value: 4.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018403  146 PVDEETFLKAAVEGK----MKVIEKFLADGGSADTCdqfrrtaLHRASLEGHM---EILEKLLDNG------------AT 206
Cdd:TIGR00870  50 RLGRSALFVAAIENEnlelTELLLNLSCRGAVGDTL-------LHAISLEYVDaveAILLHLLAAFrksgplelandqYT 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018403  207 VDFQdrLDCTAMHWACRGGHLEVVKLLQSHGADTNVR--------DKEGDTALHDAVRLNRYK------IIKLLLLHGAD 272
Cdd:TIGR00870 123 SEFT--PGITALHLAAHRQNYEIVKLLLERGASVPARacgdffvkSQGVDSFYHGESPLNAAAclgspsIVALLSEDPAD 200


                  ...
gi 194018403  273 MMT 275
Cdd:TIGR00870 201 ILT 203
PHA02741 PHA02741
hypothetical protein; Provisional
 227-288 5.57e-03

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 36.94  E-value: 5.57e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194018403 227 LEVVKLLQSHGADTNVRDK-EGDTALHDAVRLNRYKIIKLLLLH-GADMMTKNLAGKTPTDLVQ 288
Cdd:PHA02741  77 AEIIDHLIELGADINAQEMlEGDTALHLAAHRRDHDLAEWLCCQpGIDLHFCNADNKSPFELAI 140
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 182-208 5.72e-03

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: 33.77  E-value: 5.72e-03
                          10        20
                  ....*....|....*....|....*..
gi 194018403  182 RTALHRASLEGHMEILEKLLDNGATVD 208
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADIN 29
PHA02946 PHA02946
ankyin-like protein; Provisional
 218-283 7.34e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 38.11  E-value: 7.34e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194018403 218 MHWAC--RGGHLEVVKLLQSHGADTNVRDKEGDTALHDAVRLNRYKIIKLLLLHGADMMTKNLAGKTP 283
Cdd:PHA02946  41 LHAYCgiKGLDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTP 108
 
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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