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Conserved domains on  [gi|1039758020|ref|XP_017173753|]
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ankyrin repeat domain-containing protein 2 isoform X1 [Mus musculus]

Protein Classification

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

ankyrin repeat (ANK) domain-containing protein is involved in mediating protein-protein interactions

Gene Ontology:  GO:0005515
PubMed:  33435370|17176038

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
73-259 1.31e-34

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 126.99  E-value: 1.31e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039758020  73 LDLRREIIDVGGIQNLIELRKKRKQKKRDALAAAQEPPPEPEEITGPVNEETFLKAAVEGKMKVIDKYLADGGSADTCDE 152
Cdd:COG0666    39 LLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDK 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039758020 153 FRRTALHRASLEGHMEILEKLLENGATVDFQDRLDCTAMHWACRGGHLEVVRLLQSRGADTNVRDKEGDSALHDAVRLNR 232
Cdd:COG0666   119 DGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGH 198

                         170       180
                  ....*....|....*....|....*..
gi 1039758020 233 YKIIKLLLLHGADMMAKNLAGKTPTDL 259
Cdd:COG0666   199 LEIVKLLLEAGADVNAKDNDGKTALDL 225
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
73-259 1.31e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 126.99  E-value: 1.31e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039758020  73 LDLRREIIDVGGIQNLIELRKKRKQKKRDALAAAQEPPPEPEEITGPVNEETFLKAAVEGKMKVIDKYLADGGSADTCDE 152
Cdd:COG0666    39 LLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDK 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039758020 153 FRRTALHRASLEGHMEILEKLLENGATVDFQDRLDCTAMHWACRGGHLEVVRLLQSRGADTNVRDKEGDSALHDAVRLNR 232
Cdd:COG0666   119 DGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGH 198

                         170       180
                  ....*....|....*....|....*..
gi 1039758020 233 YKIIKLLLLHGADMMAKNLAGKTPTDL 259
Cdd:COG0666   199 LEIVKLLLEAGADVNAKDNDGKTALDL 225
Ank_2 pfam12796
Ankyrin repeats (3 copies);
158-250 8.30e-24

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.49  E-value: 8.30e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039758020 158 LHRASLEGHMEILEKLLENGATVDFQDRLDCTAMHWACRGGHLEVVRLLQSRgADTNVRDkEGDSALHDAVRLNRYKIIK 237
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1039758020 238 LLLLHGADMMAKN 250
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 133-258 1.05e-18

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 85.85  E-value: 1.05e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039758020 133 KMKVIDKYLADGGSADTCDEFRRTALH---RASLEGHMEILEKLLENGATVDFQDRLDCTAMH-WACRGGHLEVVRLLQS 208
Cdd:PHA03095   26 TVEEVRRLLAAGADVNFRGEYGKTPLHlylHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIK 105

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039758020 209 RGADTNVRDKEGDSALHdaVRLN----RYKIIKLLLLHGADMMAKNLAGKTPTD 258
Cdd:PHA03095  106 AGADVNAKDKVGRTPLH--VYLSgfniNPKVIRLLLRKGADVNALDLYGMTPLA 157
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 120-256 6.55e-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: 53.48  E-value: 6.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039758020 120 VNEETFLKAAVEGKMKVIDKYLadggSADTCDEFRR-----TALHRASLEGHMEILEKLLENG-------ATVDFQdrLD 187
Cdd:cd22192    16 ISESPLLLAAKENDVQAIKKLL----KCPSCDLFQRgalgeTALHVAALYDNLEAAVVLMEAApelvnepMTSDLY--QG 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039758020 188 CTAMHWACRGGHLEVVRLLQSRGADTN---------VRDKE-----GDSALHDAVRLNRYKIIKLLLLHGADMMAKNLAG 253
Cdd:cd22192    90 ETALHIAVVNQNLNLVRELIARGADVVspratgtffRPGPKnliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLG 169


                  ...
gi 1039758020 254 KTP 256
Cdd:cd22192   170 NTV 172
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 187-215 8.40e-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: 41.80  E-value: 8.40e-06
                           10        20
                   ....*....|....*....|....*....
gi 1039758020  187 DCTAMHWACRGGHLEVVRLLQSRGADTNV 215
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 122-249 5.49e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 41.61  E-value: 5.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039758020 122 EETFLKAAVEGKMKVIDKYLADGGSA--DTCDEFRRTALHRASLEG-HMEILEKLLENGATVDFQDrldcTAMHWACrgg 198
Cdd:TIGR00870  18 EKAFLPAAERGDLASVYRDLEEPKKLniNCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAVGD----TLLHAIS--- 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039758020 199 hLEVVR--------LLQSRGADTN---VRDKEGD------SALHDAVRLNRYKIIKLLLLHGADMMAK 249
Cdd:TIGR00870  91 -LEYVDaveaillhLLAAFRKSGPlelANDQYTSeftpgiTALHLAAHRQNYEIVKLLLERGASVPAR 157
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
73-259 1.31e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 126.99  E-value: 1.31e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039758020  73 LDLRREIIDVGGIQNLIELRKKRKQKKRDALAAAQEPPPEPEEITGPVNEETFLKAAVEGKMKVIDKYLADGGSADTCDE 152
Cdd:COG0666    39 LLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDK 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039758020 153 FRRTALHRASLEGHMEILEKLLENGATVDFQDRLDCTAMHWACRGGHLEVVRLLQSRGADTNVRDKEGDSALHDAVRLNR 232
Cdd:COG0666   119 DGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGH 198

                         170       180
                  ....*....|....*....|....*..
gi 1039758020 233 YKIIKLLLLHGADMMAKNLAGKTPTDL 259
Cdd:COG0666   199 LEIVKLLLEAGADVNAKDNDGKTALDL 225
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
73-256 6.41e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 120.06  E-value: 6.41e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039758020  73 LDLRREIIDVGGIQNLIELRKKRKQKKRDALAAAQEPPPEPEEITGPVNEETFLKAAVEGKMKVIDKYLADGGSADTCDE 152
Cdd:COG0666     6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039758020 153 FRRTALHRASLEGHMEILEKLLENGATVDFQDRLDCTAMHWACRGGHLEVVRLLQSRGADTNVRDKEGDSALHDAVRLNR 232
Cdd:COG0666    86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165

                         170       180
                  ....*....|....*....|....
gi 1039758020 233 YKIIKLLLLHGADMMAKNLAGKTP 256
Cdd:COG0666   166 LEIVKLLLEAGADVNARDNDGETP 189
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
128-259 7.98e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 114.28  E-value: 7.98e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039758020 128 AAVEGKMKVIDKYLADGGSADTCDEFRRTALHRASLEGHMEILEKLLENGATVDFQDRLDCTAMHWACRGGHLEVVRLLQ 207
Cdd:COG0666   127 AAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLL 206

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039758020 208 SRGADTNVRDKEGDSALHDAVRLNRYKIIKLLLLHGADMMAKNLAGKTPTDL 259
Cdd:COG0666   207 EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLL 258
Ank_2 pfam12796
Ankyrin repeats (3 copies);
158-250 8.30e-24

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.49  E-value: 8.30e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039758020 158 LHRASLEGHMEILEKLLENGATVDFQDRLDCTAMHWACRGGHLEVVRLLQSRgADTNVRDkEGDSALHDAVRLNRYKIIK 237
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1039758020 238 LLLLHGADMMAKN 250
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 133-258 1.05e-18

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 85.85  E-value: 1.05e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039758020 133 KMKVIDKYLADGGSADTCDEFRRTALH---RASLEGHMEILEKLLENGATVDFQDRLDCTAMH-WACRGGHLEVVRLLQS 208
Cdd:PHA03095   26 TVEEVRRLLAAGADVNFRGEYGKTPLHlylHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIK 105

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039758020 209 RGADTNVRDKEGDSALHdaVRLN----RYKIIKLLLLHGADMMAKNLAGKTPTD 258
Cdd:PHA03095  106 AGADVNAKDKVGRTPLH--VYLSgfniNPKVIRLLLRKGADVNALDLYGMTPLA 157
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
128-255 5.91e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 81.92  E-value: 5.91e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039758020 128 AAVEGKMKVIDKYLADGGSADTCDEFRRTALHRASLEGHMEILEKLLENGATVDFQDRLDCTAMHWACRGGHLEVVRLLQ 207
Cdd:COG0666   160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1039758020 208 SRGADTNVRDKEGDSALHDAVRLNRYKIIKLLLLHGADMMAKNLAGKT 255
Cdd:COG0666   240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
Ank_2 pfam12796
Ankyrin repeats (3 copies);
128-217 6.16e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.38  E-value: 6.16e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039758020 128 AAVEGKMKVIDKYLADGGSADTCDEFRRTALHRASLEGHMEILEKLLENgATVDFQDRlDCTAMHWACRGGHLEVVRLLQ 207
Cdd:pfam12796   4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLL 81

                          90
                  ....*....|
gi 1039758020 208 SRGADTNVRD 217
Cdd:pfam12796  82 EKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 136-256 1.38e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 76.54  E-value: 1.38e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039758020 136 VIDKYLADGGSADTCDEFRRTALHRASLEGHMEILEKLLENGATVDFQDRLDCTAMHWACRGGHLEVVRLLQSRGADTNV 215
Cdd:PHA02874  106 MIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANV 185

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1039758020 216 RDKEGDSALHDAVRLNRYKIIKLLLLHGADMMAKNLAGKTP 256
Cdd:PHA02874  186 KDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTP 226
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 168-256 1.64e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 70.38  E-value: 1.64e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039758020 168 EILEKLLENGATVDFQDRLDCTAMHWACRGGHLEVVRLLQSRGADTNVRDKEGDSALHDAVRLNRYKIIKLLLLHGADMM 247
Cdd:PHA02874  105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184


                  ....*....
gi 1039758020 248 AKNLAGKTP 256
Cdd:PHA02874  185 VKDNNGESP 193
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 133-250 3.27e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 69.31  E-value: 3.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039758020 133 KMKVIDKYLADGGSADTCDEFRRTALHRASLEGH-----MEILEKLLENGATVDFQDRLDCTAMHWA--CRGGHLEVVRL 205
Cdd:PHA03100   47 NIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITPLLYAisKKSNSYSIVEY 126

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1039758020 206 LQSRGADTNVRDKEGDSALHDAVRLNRY--KIIKLLLLHGADMMAKN 250
Cdd:PHA03100  127 LLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKN 173
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 135-250 1.65e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 67.21  E-value: 1.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039758020 135 KVIDKYLADGGSADTCDEFR-RTALHRASLEGHMEILEKLLENGATVDFQDRLDCTAMHWACRGGHLEVVRLLQSRGADT 213
Cdd:PHA02878  148 EITKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAST 227

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1039758020 214 NVRDKEGDSALHDAV-RLNRYKIIKLLLLHGADMMAKN 250
Cdd:PHA02878  228 DARDKCGNTPLHISVgYCKDYDILKLLLEHGVDVNAKS 265
Ank_4 pfam13637
Ankyrin repeats (many copies);
154-206 2.93e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 60.37  E-value: 2.93e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039758020 154 RRTALHRASLEGHMEILEKLLENGATVDFQDRLDCTAMHWACRGGHLEVVRLL 206
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 168-256 8.78e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 65.29  E-value: 8.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039758020 168 EILEKLLENGATVDFQDR-LDCTAMHWACRGGHLEVVRLLQSRGADTNVRDKEGDSALHDAVRLNRYKIIKLLLLHGADM 246
Cdd:PHA02878  148 EITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAST 227

                          90
                  ....*....|
gi 1039758020 247 MAKNLAGKTP 256
Cdd:PHA02878  228 DARDKCGNTP 237
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 141-256 1.10e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 62.00  E-value: 1.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039758020 141 LADGG-SADTCDEFRRTALHRASLEGHM-EILEKLLENGATVDFQDRLDCTAMHWACRGGH-LEVVRLLQSRGADTNVRD 217
Cdd:PHA02876  259 LYDAGfSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAAD 338

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1039758020 218 KEGDSALHDAVRLNRYKIIKLLLLH-GADMMAKNLAGKTP 256
Cdd:PHA02876  339 RLYITPLHQASTLDRNKDIVITLLElGANVNARDYCDKTP 378
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 137-245 1.61e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 61.22  E-value: 1.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039758020 137 IDKYLADGGS---ADTCDEFrrTALHrASLEG---HMEILEKLLENGATVDFQDRLDC----------------TAMHWA 194
Cdd:PHA03100  123 IVEYLLDNGAnvnIKNSDGE--NLLH-LYLESnkiDLKILKLLIDKGVDINAKNRVNYllsygvpinikdvygfTPLHYA 199

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039758020 195 CRGGHLEVVRLLQSRGADTNVRDKEGDSALHDAVRLNRYKIIKLLLLHGAD 245
Cdd:PHA03100  200 VYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 134-245 2.87e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 60.39  E-value: 2.87e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039758020 134 MKVIDKYLADggsADTCDEFRRTALHRASLEGHMEILEKLLENGATVDFQDRLDCTAMHWACRGGHLEVVRLLQSRGADT 213
Cdd:PHA02875  118 MKLLIARGAD---PDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANI 194

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1039758020 214 NVRDKEGD-SALHDAVRLNRYKIIKLLLLHGAD 245
Cdd:PHA02875  195 DYFGKNGCvAALCYAIENNKIDIVRLFIKRGAD 227
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 167-256 3.46e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 60.06  E-value: 3.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039758020 167 MEILEKLLENGATVDFQDRLDCTAMHWACRGGH-----LEVVRLLQSRGADTNVRDKEGDSALHDAV--RLNRYKIIKLL 239
Cdd:PHA03100   48 IDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYL 127

                          90
                  ....*....|....*..
gi 1039758020 240 LLHGADMMAKNLAGKTP 256
Cdd:PHA03100  128 LDNGANVNIKNSDGENL 144
PHA03095 PHA03095
ankyrin-like protein; Provisional
 135-256 7.61e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 59.27  E-value: 7.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039758020 135 KVIDKYLADGGSADTCDEFRRTALHR--ASLEGHMEILEKLLENGATVDFQDRLDCTAMHWACR--GGHLEVVRLLQSRG 210
Cdd:PHA03095   98 DVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKsrNANVELLRLLIDAG 177

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1039758020 211 ADTNVRDKEGDSALH---DAVRlNRYKIIKLLLLHGADMMAKNLAGKTP 256
Cdd:PHA03095  178 ADVYAVDDRFRSLLHhhlQSFK-PRARIVRELIRAGCDPAATDMLGNTP 225
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
134-256 7.86e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 58.43  E-value: 7.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039758020 134 MKVIDKYLADGGSADTCDEFRRTALHRASLEGHMEILEKLLENGATVDFQDRLDCTAMHWACRGGHLEVVRLLQSRGADT 213
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1039758020 214 NVRDKEGDSALHDAVRLNRYKIIKLLLLHGADMMAKNLAGKTP 256
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETP 123
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 134-256 8.17e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 59.29  E-value: 8.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039758020 134 MKVIDKYLADGGSADTCDEFRRTALHRASLE--GHMEILEKLLENGATVDFQDRLDCTAMHWACRGGH--LEVVRLLQSR 209
Cdd:PHA03100   86 KEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDK 165

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039758020 210 GAD----------------TNVRDKEGDSALHDAVRLNRYKIIKLLLLHGADMMAKNLAGKTP 256
Cdd:PHA03100  166 GVDinaknrvnyllsygvpINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTP 228
Ank_4 pfam13637
Ankyrin repeats (many copies);
189-240 1.30e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.05  E-value: 1.30e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039758020 189 TAMHWACRGGHLEVVRLLQSRGADTNVRDKEGDSALHDAVRLNRYKIIKLLL 240
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 155-256 3.68e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 57.31  E-value: 3.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039758020 155 RTALHRASLEGHMEILEKLLENGATVD---FQDRLdcTAMHWACRGGHLEVVRLLQSRGADTNVRDKEGDSALHDAVRLN 231
Cdd:PHA02875   69 ESELHDAVEEGDVKAVEELLDLGKFADdvfYKDGM--TPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMG 146

                          90       100
                  ....*....|....*....|....*
gi 1039758020 232 RYKIIKLLLLHGADMMAKNLAGKTP 256
Cdd:PHA02875  147 DIKGIELLIDHKACLDIEDCCGCTP 171
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 144-256 5.64e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 57.00  E-value: 5.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039758020 144 GGSADTCDEFRRTALHRASLEGHMEILEKLLENGATVDFQDRLDCTAMHWACRGGH-LEVVRLLQSRGADTNVRDKEGDS 222
Cdd:PHA02876  365 GANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNpYMSVKTLIDRGANVNSKNKDLST 444

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1039758020 223 ALHDAVRLN-RYKIIKLLLLHGADMMAKNLAGKTP 256
Cdd:PHA02876  445 PLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYP 479
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 173-275 8.99e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.45  E-value: 8.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039758020 173 LLENGATVDFQDRLDCTAMHWACRGGHLEVVRLLQSRGADTNVRDKEGDSALHDAVRLNRYKIIKLLLLH-------GAD 245
Cdd:PTZ00322  101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHsqchfelGAN 180

                          90       100       110
                  ....*....|....*....|....*....|
gi 1039758020 246 MMAKNLAGKTPTdlvqlwQADTRHALEHPE 275
Cdd:PTZ00322  181 AKPDSFTGKPPS------LEDSPISSHHPD 204
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 124-260 1.06e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 55.66  E-value: 1.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039758020 124 TFLKAAVEGKMKVIDKYL----ADGGSADTCDefrRTALHRASLEGHMEILEKLLENGATVDFQDRLDCTAMHWAC-RGG 198
Cdd:PHA02878  170 TALHYATENKDQRLTELLlsygANVNIPDKTN---NSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVgYCK 246

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039758020 199 HLEVVRLLQSRGADTNVRDK-EGDSALHDAVRLNRykIIKLLLLHGADMMAKNLAGKTPTDLV 260
Cdd:PHA02878  247 DYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSER--KLKLLLEYGADINSLNSYKLTPLSSA 307
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 117-264 2.87e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.87  E-value: 2.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039758020 117 TGPVNEETFLKAAVEGKMKVIDKYLADGGSADTCDEFRRTALHRASLEGHMEILEKLLENGATVDFQDRLDCTAMhW--- 193
Cdd:PLN03192  521 DDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTAL-Wnai 599

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039758020 194 -----------------------------ACRGGHLEVVRLLQSRGADTNVRDKEGDSALHDAVRLNRYKIIKLLLLHGA 244
Cdd:PLN03192  600 sakhhkifrilyhfasisdphaagdllctAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGA 679

                         170       180
                  ....*....|....*....|.
gi 1039758020 245 DMMAKNLAGK-TPTDLVQLWQ 264
Cdd:PLN03192  680 DVDKANTDDDfSPTELRELLQ 700
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 123-274 4.93e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.81  E-value: 4.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039758020 123 ETFLKAAVE-GKMKVIDKYLADGGSADTCDEFRRTALHRASLEGHMEILEKLLENGATVDFQDRLDCTAMHWACRGGHLE 201
Cdd:PHA02874  125 KTFLHYAIKkGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYA 204

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039758020 202 VVRLLQSRGADTNVRDKEGDSALHDAVRLNRYKIikLLLLHGADMMAKNLAGKTPtdlvqlwqadTRHALEHP 274
Cdd:PHA02874  205 CIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAI--ELLINNASINDQDIDGSTP----------LHHAINPP 265
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 120-256 6.55e-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: 53.48  E-value: 6.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039758020 120 VNEETFLKAAVEGKMKVIDKYLadggSADTCDEFRR-----TALHRASLEGHMEILEKLLENG-------ATVDFQdrLD 187
Cdd:cd22192    16 ISESPLLLAAKENDVQAIKKLL----KCPSCDLFQRgalgeTALHVAALYDNLEAAVVLMEAApelvnepMTSDLY--QG 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039758020 188 CTAMHWACRGGHLEVVRLLQSRGADTN---------VRDKE-----GDSALHDAVRLNRYKIIKLLLLHGADMMAKNLAG 253
Cdd:cd22192    90 ETALHIAVVNQNLNLVRELIARGADVVspratgtffRPGPKnliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLG 169


                  ...
gi 1039758020 254 KTP 256
Cdd:cd22192   170 NTV 172
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 125-239 1.27e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 52.95  E-value: 1.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039758020 125 FLKAAVEGKMKVIDKYLADGGSADTCDEFRRTALHRASLeGHMEILEKLLENGATVDFQDRLDCTAMHWACRGGHLEVVR 204
Cdd:PLN03192  497 FLQHHKELHDLNVGDLLGDNGGEHDDPNMASNLLTVAST-GNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVL 575

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1039758020 205 LLQSRGADTNVRDKEGDSALHDAVRLNRYKIIKLL 239
Cdd:PLN03192  576 VLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 144-256 1.55e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 52.37  E-value: 1.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039758020 144 GGSADTCDEFRRTALHRAS-LEGHMEILEKLLENGATVDFQDRLDCTAMHWACRGGHLEVVRLLQSRGADTNVRDKEGDS 222
Cdd:PHA02876  331 GADVNAADRLYITPLHQAStLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGT 410

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1039758020 223 ALHDAV-RLNRYKIIKLLLLHGADMMAKNLAGKTP 256
Cdd:PHA02876  411 ALHFALcGTNPYMSVKTLIDRGANVNSKNKDLSTP 445
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 153-278 2.56e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.82  E-value: 2.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039758020 153 FRRTALHR---ASLEGHMEILEKLLENGATVDF----QDRLDCTAMHWA----CR---GGHLEVVRLLQSRGADTNVRDK 218
Cdd:PTZ00322   34 FERMAAIQeeiARIDTHLEALEATENKDATPDHnlttEEVIDPVVAHMLtvelCQlaaSGDAVGARILLTGGADPNCRDY 113

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039758020 219 EGDSALHDAVRLNRYKIIKLLLLHGADMMAKNLAGKTPTDLV------QLWQADTRHALEHPEPES 278
Cdd:PTZ00322  114 DGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAeengfrEVVQLLSRHSQCHFELGA 179
Ank_5 pfam13857
Ankyrin repeats (many copies);
173-225 5.04e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.80  E-value: 5.04e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039758020 173 LLENG-ATVDFQDRLDCTAMHWACRGGHLEVVRLLQSRGADTNVRDKEGDSALH 225
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 128-256 4.68e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 47.68  E-value: 4.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039758020 128 AAVEGKMKVIDKYLADGGSADtcDEFRR---TALHRASLEGHMEILEKLLENGATVDFQDRLDCTAMHWACRGGHLEVVR 204
Cdd:PHA02875   75 AVEEGDVKAVEELLDLGKFAD--DVFYKdgmTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIE 152

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039758020 205 LLQSRGADTNVRDKEGDSALHDAVRLNRYKIIKLLLLHGADMmakNLAGKTP 256
Cdd:PHA02875  153 LLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANI---DYFGKNG 201
PHA03095 PHA03095
ankyrin-like protein; Provisional
 135-240 6.70e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 47.33  E-value: 6.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039758020 135 KVIDKYLADGGSADTCDEFRRTALHRASLEGHME--ILEKLLENGATVDFQDRLDCTAMHWA-CRGGHLEVVRLLQsRGA 211
Cdd:PHA03095  203 RIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPLHYAaVFNNPRACRRLIA-LGA 281

                          90       100
                  ....*....|....*....|....*....
gi 1039758020 212 DTNVRDKEGDSALHDAVRLNRYKIIKLLL 240
Cdd:PHA03095  282 DINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
Ank_5 pfam13857
Ankyrin repeats (many copies);
205-260 7.06e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.72  E-value: 7.06e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039758020 205 LLQSRGADTNVRDKEGDSALHDAVRLNRYKIIKLLLLHGADMMAKNLAGKTPTDLV 260
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 187-215 8.40e-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: 41.80  E-value: 8.40e-06
                           10        20
                   ....*....|....*....|....*....
gi 1039758020  187 DCTAMHWACRGGHLEVVRLLQSRGADTNV 215
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
123-174 8.96e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.26  E-value: 8.96e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039758020 123 ETFLKAAVEGKMKVIDKYLADGGSADTCDEFRRTALHRASLEGHMEILEKLL 174
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 188-218 1.08e-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: 41.51  E-value: 1.08e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1039758020 188 CTAMHWAC-RGGHLEVVRLLQSRGADTNVRDK 218
Cdd:pfam00023   3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 164-252 1.60e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.21  E-value: 1.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039758020 164 EGHMEILEKLLENGATVDFQDRLDCTAMHWACRGGHLEVVRLLQSRGADTNVRDKEGDSALHDAVRLNRYKIIKLLLLHG 243
Cdd:PHA02876  155 QDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNR 234


                  ....*....
gi 1039758020 244 ADMMAKNLA 252
Cdd:PHA02876  235 SNINKNDLS 243
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 141-208 3.03e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 45.27  E-value: 3.03e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039758020 141 LADGGSADTCDEFRRTALHRASLEGHMEILEKLLENGATVDFQDRLDCTAMHWACRGGHLEVVRLLQS 208
Cdd:PTZ00322  102 LTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 128-215 4.64e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 44.60  E-value: 4.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039758020 128 AAVEGKMKVIDKYLADGGSADTCDEFRRTALHRASLEGHMEILEKLLENGATVD-FQDRLDCTAMHWACRGGHLEVVRLL 206
Cdd:PHA02875  142 AVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDyFGKNGCVAALCYAIENNKIDIVRLF 221


                  ....*....
gi 1039758020 207 QSRGADTNV 215
Cdd:PHA02875  222 IKRGADCNI 230
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
128-224 7.94e-05

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 43.40  E-value: 7.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039758020 128 AAVEGKMKVIDKYLADGGSADTCDEFRRTALHRASLEGHMEILEKLLENGATVDFQDRLDCTAMHWACRGGHLEVVRLLQ 207
Cdd:COG0666   193 AAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLL 272

                          90
                  ....*....|....*..
gi 1039758020 208 SRGADTNVRDKEGDSAL 224
Cdd:COG0666   273 LALLLLAAALLDLLTLL 289
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 155-264 2.27e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 42.29  E-value: 2.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039758020 155 RTALHRASLEGHMEILEKLLENGATVDFQDRLDCTAMHWACRGGHLEVVRLLQSRGADTNVRDKEGDSALHDAVRLNRYK 234
Cdd:PHA02875    3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1039758020 235 IIKLLLLHGA---DMMAKNlaGKTPTDLVQLWQ 264
Cdd:PHA02875   83 AVEELLDLGKfadDVFYKD--GMTPLHLATILK 113
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 189-215 3.80e-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: 3.80e-04
                          10        20
                  ....*....|....*....|....*..
gi 1039758020 189 TAMHWACRGGHLEVVRLLQSRGADTNV 215
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADINA 30
PHA02946 PHA02946
ankyin-like protein; Provisional
 191-256 4.24e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 41.58  E-value: 4.24e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039758020 191 MHWAC--RGGHLEVVRLLQSRGADTNVRDKEGDSALHDAVRLNRYKIIKLLLLHGADMMAKNLAGKTP 256
Cdd:PHA02946   41 LHAYCgiKGLDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTP 108
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 155-181 4.57e-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: 36.80  E-value: 4.57e-04
                           10        20
                   ....*....|....*....|....*..
gi 1039758020  155 RTALHRASLEGHMEILEKLLENGATVD 181
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 121-256 4.58e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 41.49  E-value: 4.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039758020 121 NEETFLKAAVE-GKMKVIdKYLADGGS--ADTCDEfRRTALHRASLEGHMEIleKLLENGATVDFQDRLDCTAMHWA--- 194
Cdd:PHA02874  189 NGESPLHNAAEyGDYACI-KLLIDHGNhiMNKCKN-GFTPLHNAIIHNRSAI--ELLINNASINDQDIDGSTPLHHAinp 264

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039758020 195 -CrggHLEVVRLLQSRGADTNVRDKEGDSALHDAVR-LNRYKIIKLLLlhgADMMAKNLAGKTP 256
Cdd:PHA02874  265 pC---DIDIIDILLYHKADISIKDNKGENPIDTAFKyINKDPVIKDII---ANAVLIKEADKLK 322
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 219-250 4.84e-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: 36.88  E-value: 4.84e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1039758020 219 EGDSALHDAV-RLNRYKIIKLLLLHGADMMAKN 250
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 135-242 5.43e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 41.40  E-value: 5.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039758020 135 KVIDKYLADGGSADTCDEFRRTALHRASleGHM---EILEKLLENGATVDFQDR-LDCTAMHWACRGGhlEVVRLLQSRG 210
Cdd:PHA02878  215 PIVHILLENGASTDARDKCGNTPLHISV--GYCkdyDILKLLLEHGVDVNAKSYiLGLTALHSSIKSE--RKLKLLLEYG 290

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1039758020 211 ADTNVRDKEGDSALHDAVRLNR-YKIIKLLLLH 242
Cdd:PHA02878  291 ADINSLNSYKLTPLSSAVKQYLcINIGRILISN 323
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 122-249 5.49e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 41.61  E-value: 5.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039758020 122 EETFLKAAVEGKMKVIDKYLADGGSA--DTCDEFRRTALHRASLEG-HMEILEKLLENGATVDFQDrldcTAMHWACrgg 198
Cdd:TIGR00870  18 EKAFLPAAERGDLASVYRDLEEPKKLniNCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAVGD----TLLHAIS--- 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039758020 199 hLEVVR--------LLQSRGADTN---VRDKEGD------SALHDAVRLNRYKIIKLLLLHGADMMAK 249
Cdd:TIGR00870  91 -LEYVDaveaillhLLAAFRKSGPlelANDQYTSeftpgiTALHLAAHRQNYEIVKLLLERGASVPAR 157
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 201-256 7.50e-04

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 39.47  E-value: 7.50e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039758020 201 EVVRLLQSRGADTNVRD-KEGDSALHDAVRLNRYKIIKLLLLH-GADMMAKNLAGKTP 256
Cdd:PHA02736   72 EKLKLLMEWGADINGKErVFGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTP 129
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 131-260 1.04e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 40.43  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039758020 131 EGKMKVIDKYLADGGSADTCDEFRRTALHRASLEGHMEILEKLLENGATVDFQDRLDCTAMHWAC--------------- 195
Cdd:PHA02876  155 QDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVdsknidtikaiidnr 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039758020 196 --------------RGGHLEVVRLLQSRGADTNVRDKEGDSALHDAVRL-NRYKIIKLLLLHGADMMAKNLAGKTPTDLV 260
Cdd:PHA02876  235 sninkndlsllkaiRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIKGETPLYLM 314
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 155-185 1.05e-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: 36.11  E-value: 1.05e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1039758020 155 RTALHRASLE-GHMEILEKLLENGATVDFQDR 185
Cdd:pfam00023   3 NTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 219-246 1.13e-03

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: 35.64  E-value: 1.13e-03
                           10        20
                   ....*....|....*....|....*...
gi 1039758020  219 EGDSALHDAVRLNRYKIIKLLLLHGADM 246
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 165-245 1.40e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 39.95  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039758020 165 GHMEILEKLLEN-GATVDFQDRLDCTAMHWACRGGHLEVVRLLQSRGADTNVRDKEGDSALHDAVRLNRYKIIKLLLLHG 243
Cdd:PHA02874   12 GDIEAIEKIIKNkGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG 91


                  ..
gi 1039758020 244 AD 245
Cdd:PHA02874   92 VD 93
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 155-181 1.89e-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: 35.31  E-value: 1.89e-03
                          10        20
                  ....*....|....*....|....*..
gi 1039758020 155 RTALHRASLEGHMEILEKLLENGATVD 181
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADIN 29
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 219-245 4.48e-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: 34.16  E-value: 4.48e-03
                          10        20
                  ....*....|....*....|....*..
gi 1039758020 219 EGDSALHDAVRLNRYKIIKLLLLHGAD 245
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGAD 27
PHA02917 PHA02917
ankyrin-like protein; Provisional
 212-255 7.15e-03

ankyrin-like protein; Provisional


Pssm-ID: 165231 [Multi-domain]  Cd Length: 661  Bit Score: 38.06  E-value: 7.15e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1039758020 212 DTNVRDKEGDSALHDAVRLNRYKIIKLLLLHGADMMAKNLAGKT 255
Cdd:PHA02917  444 DINMIDKRGETLLHKAVRYNKQSLVSLLLESGSDVNIRSNNGYT 487
 
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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