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Conserved domains on  [gi|19921360|ref|NP_609735|]
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Ankrd49 [Drosophila melanogaster]

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];
52-194 1.46e-30

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 113.90  E-value: 1.46e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921360  52 ILWAVNENRISEVREILKLDADtVNAKDNDGYTPLHRAAYNNFVDMAKLLLQYHANPNARTELGWTPLHSACKWNNADCA 131
Cdd:COG0666  91 LHAAARNGDLEIVKLLLEAGAD-VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19921360 132 HLLLQFGADVNAESDGKQTPLHItATVSNcrNTATV-LLLDRYIQPRKENNSEELASVIARRTG 194
Cdd:COG0666 170 KLLLEAGADVNARDNDGETPLHL-AAENG--HLEIVkLLLEAGADVNAKDNDGKTALDLAAENG 230
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
52-194 1.46e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 113.90  E-value: 1.46e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921360  52 ILWAVNENRISEVREILKLDADtVNAKDNDGYTPLHRAAYNNFVDMAKLLLQYHANPNARTELGWTPLHSACKWNNADCA 131
Cdd:COG0666  91 LHAAARNGDLEIVKLLLEAGAD-VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19921360 132 HLLLQFGADVNAESDGKQTPLHItATVSNcrNTATV-LLLDRYIQPRKENNSEELASVIARRTG 194
Cdd:COG0666 170 KLLLEAGADVNARDNDGETPLHL-AAENG--HLEIVkLLLEAGADVNAKDNDGKTALDLAAENG 230
Ank_2 pfam12796
Ankyrin repeats (3 copies);
52-143 3.92e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 83.63  E-value: 3.92e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921360    52 ILWAVNENRISEVREILKLDADtVNAKDNDGYTPLHRAAYNNFVDMAKLLLQyHANPNARTElGWTPLHSACKWNNADCA 131
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGAD-ANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIV 77

                          90
                  ....*....|..
gi 19921360   132 HLLLQFGADVNA 143
Cdd:pfam12796  78 KLLLEKGADINV 89
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 48-143 2.26e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 79.71  E-value: 2.26e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921360   48 IERMILWAVNENRISEVREILKLDADtVNAKDNDGYTPLHRAAYNNFVDMAKLLLQYHANPNARTELGWTPLHSACKWNN 127
Cdd:PHA03100 159 LKLLIDKGVDINAKNRVNYLLSYGVP-INIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNN 237

                         90
                 ....*....|....*.
gi 19921360  128 ADCAHLLLQFGADVNA 143
Cdd:PHA03100 238 KEIFKLLLNNGPSIKT 253
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 115-143 7.36e-07

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: 44.12  E-value: 7.36e-07
                           10        20
                   ....*....|....*....|....*....
gi 19921360    115 GWTPLHSACKWNNADCAHLLLQFGADVNA 143
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 84-197 3.00e-04

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: 41.15  E-value: 3.00e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921360  84 TPLHRAAYNNFVD-MAKLLLQYHANPNARTELGWTPLHSACKWNNADCAHLLLQFGAD-VNAE--SD---GkQTPLHItA 156
Cdd:cd22192  19 SPLLLAAKENDVQaIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPmtSDlyqG-ETALHI-A 96

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 19921360 157 TVSNcrNTATV-LLLDRYiqprkennseelASVI-ARRTGMSF 197
Cdd:cd22192  97 VVNQ--NLNLVrELIARG------------ADVVsPRATGTFF 125
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 35-143 3.35e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 41.22  E-value: 3.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921360    35 DELIEEDKNPQSSIERM----ILWAVNENRISEVREILKLdadtvnaKDNDGY---TPLHrAAYNNFVDMAKLLLQY--- 104
Cdd:TIGR00870  35 RDLEEPKKLNINCPDRLgrsaLFVAAIENENLELTELLLN-------LSCRGAvgdTLLH-AISLEYVDAVEAILLHlla 106

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 19921360   105 ---------HANPNARTEL--GWTPLHSACKWNNADCAHLLLQFGADVNA 143
Cdd:TIGR00870 107 afrksgpleLANDQYTSEFtpGITALHLAAHRQNYEIVKLLLERGASVPA 156
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
52-194 1.46e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 113.90  E-value: 1.46e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921360  52 ILWAVNENRISEVREILKLDADtVNAKDNDGYTPLHRAAYNNFVDMAKLLLQYHANPNARTELGWTPLHSACKWNNADCA 131
Cdd:COG0666  91 LHAAARNGDLEIVKLLLEAGAD-VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19921360 132 HLLLQFGADVNAESDGKQTPLHItATVSNcrNTATV-LLLDRYIQPRKENNSEELASVIARRTG 194
Cdd:COG0666 170 KLLLEAGADVNARDNDGETPLHL-AAENG--HLEIVkLLLEAGADVNAKDNDGKTALDLAAENG 230
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
31-194 6.99e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 96.18  E-value: 6.99e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921360  31 DDDADELIEEDKNPQSSIERMILWAVNENRISEVREILKLDADTVNAKDNDGYTPLHRAAYNNFVDMAKLLLQYHANPNA 110
Cdd:COG0666  36 LLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNA 115

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921360 111 RTELGWTPLHSACKWNNADCAHLLLQFGADVNAESDGKQTPLHITATvsnCRNTATV-LLLDRYIQPRKENNSEELASVI 189
Cdd:COG0666 116 RDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA---NGNLEIVkLLLEAGADVNARDNDGETPLHL 192


                ....*
gi 19921360 190 ARRTG 194
Cdd:COG0666 193 AAENG 197
Ank_2 pfam12796
Ankyrin repeats (3 copies);
52-143 3.92e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 83.63  E-value: 3.92e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921360    52 ILWAVNENRISEVREILKLDADtVNAKDNDGYTPLHRAAYNNFVDMAKLLLQyHANPNARTElGWTPLHSACKWNNADCA 131
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGAD-ANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIV 77

                          90
                  ....*....|..
gi 19921360   132 HLLLQFGADVNA 143
Cdd:pfam12796  78 KLLLEKGADINV 89
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
52-185 2.78e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 86.55  E-value: 2.78e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921360  52 ILWAVNENRISEVREILKLDADtVNAKDNDGYTPLHRAAYNNFVDMAKLLLQYHANPNARTELGWTPLHSACKWNNADCA 131
Cdd:COG0666 157 LHLAAANGNLEIVKLLLEAGAD-VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIV 235

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 19921360 132 HLLLQFGADVNAESDGKQTPLHITATVSNCRNTATVLLLDRYIQPRKENNSEEL 185
Cdd:COG0666 236 KLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
86-169 3.24e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.62  E-value: 3.24e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921360    86 LHRAAYNNFVDMAKLLLQYHANPNARTELGWTPLHSACKWNNADCAHLLLQFgADVNAESDGKqTPLHItATVSNCRNTA 165
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGR-TALHY-AARSGHLEIV 77


                  ....
gi 19921360   166 TVLL 169
Cdd:pfam12796  78 KLLL 81
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 48-143 2.26e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 79.71  E-value: 2.26e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921360   48 IERMILWAVNENRISEVREILKLDADtVNAKDNDGYTPLHRAAYNNFVDMAKLLLQYHANPNARTELGWTPLHSACKWNN 127
Cdd:PHA03100 159 LKLLIDKGVDINAKNRVNYLLSYGVP-INIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNN 237

                         90
                 ....*....|....*.
gi 19921360  128 ADCAHLLLQFGADVNA 143
Cdd:PHA03100 238 KEIFKLLLNNGPSIKT 253
PHA03095 PHA03095
ankyrin-like protein; Provisional
 59-183 1.72e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 71.21  E-value: 1.72e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921360   59 NRISEVREILKLDADtVNAKDNDGYTPLH---RAAYNNFVDMAKLLLQYHANPNARTELGWTPLHS-ACKWNNADCAHLL 134
Cdd:PHA03095  25 VTVEEVRRLLAAGAD-VNFRGEYGKTPLHlylHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLyLYNATTLDVIKLL 103

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 19921360  135 LQFGADVNAESDGKQTPLHITATVSNCRNTATVLLLDRYIQPRKENNSE 183
Cdd:PHA03095 104 IKAGADVNAKDKVGRTPLHVYLSGFNINPKVIRLLLRKGADVNALDLYG 152
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
51-172 7.80e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 65.75  E-value: 7.80e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921360  51 MILWAVNENRISEVREILKLDADTVNAKDNDGYTPLHRAAYNNFVDMAKLLLQYHANPNARTELGWTPLHSACKWNNADC 130
Cdd:COG0666  23 LLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEI 102

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 19921360 131 AHLLLQFGADVNAESDGKQTPLHITAtvsNCRNTATV-LLLDR 172
Cdd:COG0666 103 VKLLLEAGADVNARDKDGETPLHLAA---YNGNLEIVkLLLEA 142
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 64-172 1.26e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 66.06  E-value: 1.26e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921360   64 VREILKLDADTVNAKDNDGYTPLHRAAYNNFVDMAKLLLQYHANPNARTELGWTPLHSACKWNNADCAHLLLQFGADVNA 143
Cdd:PHA02878 150 TKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229

                         90       100       110
                 ....*....|....*....|....*....|
gi 19921360  144 ESDGKQTPLHItaTVSNCRNTATV-LLLDR 172
Cdd:PHA02878 230 RDKCGNTPLHI--SVGYCKDYDILkLLLEH 257
Ank_4 pfam13637
Ankyrin repeats (many copies);
82-135 1.63e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.98  E-value: 1.63e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 19921360    82 GYTPLHRAAYNNFVDMAKLLLQYHANPNARTELGWTPLHSACKWNNADCAHLLL 135
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 54-185 1.84e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 65.37  E-value: 1.84e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921360   54 WAVNENRISEVREILKLDADtVNAKDNDGYTPLHRAAYNNFVDMAKLLLQYHANPNARTELGWTPLHSACKWNNADCAHL 133
Cdd:PHA02874 130 YAIKKGDLESIKMLFEYGAD-VNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKL 208

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 19921360  134 LLQFGADVNAESDGKQTPLHiTATVSNcRNTATVLLLDRYIQPRKENNSEEL 185
Cdd:PHA02874 209 LIDHGNHIMNKCKNGFTPLH-NAIIHN-RSAIELLINNASINDQDIDGSTPL 258
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 59-181 2.90e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 61.99  E-value: 2.90e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921360   59 NRISEVREILKLDADtVNAKDNDGYTPLHRAAYNNFVD--MAKLLLQYHANPNARTEL----------------GWTPLH 120
Cdd:PHA03100 119 NSYSIVEYLLDNGAN-VNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDINAKNRVnyllsygvpinikdvyGFTPLH 197

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19921360  121 SACKWNNADCAHLLLQFGADVNAESDGKQTPLHITATVSN-------CRNTATVLLLDRYIQPRKENN 181
Cdd:PHA03100 198 YAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNkeifkllLNNGPSIKTIIETLLYFKDKD 265
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 66-180 6.49e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 57.97  E-value: 6.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921360   66 EILKLDADTVNAKDNDGYTPLHRA-AYNNFVDMAKLLLQYHANPNARTE-LGWTPLHSACKwnNADCAHLLLQFGADVNA 143
Cdd:PHA02878 218 HILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIK--SERKLKLLLEYGADINS 295

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 19921360  144 ESDGKQTPLHITATVSNCRNTATVLL----LDRYIQPRKEN 180
Cdd:PHA02878 296 LNSYKLTPLSSAVKQYLCINIGRILIsnicLLKRIKPDIKN 336
PHA03095 PHA03095
ankyrin-like protein; Provisional
 51-182 8.87e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 57.34  E-value: 8.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921360   51 MILWAVNENRISEVREILKLDADtVNAKDNDGYTPLHRAAYNNFVD--MAKLLLQYHANPNARTELGWTPLHSACKWNNA 128
Cdd:PHA03095  87 LHLYLYNATTLDVIKLLIKAGAD-VNAKDKVGRTPLHVYLSGFNINpkVIRLLLRKGADVNALDLYGMTPLAVLLKSRNA 165

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 19921360  129 DCA--HLLLQFGADVNAESDGKQTPLHITATVSNCRNTATVLLLDRYIQPRKENNS 182
Cdd:PHA03095 166 NVEllRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRARIVRELIRAGCDPAATDML 221
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 51-172 5.82e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 55.45  E-value: 5.82e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921360   51 MILWAVNENRISEVREILKLDADtVNAKDNDGYTPLHRAA-YNNFVDMAKLLLQYHANPNARTELGWTPLHSACKWNNAD 129
Cdd:PHA02876 311 LYLMAKNGYDTENIRTLIMLGAD-VNAADRLYITPLHQAStLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVV 389

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 19921360  130 CAHLLLQFGADVNAESDGKQTPLHITATVSNcRNTATVLLLDR 172
Cdd:PHA02876 390 IINTLLDYGADIEALSQKIGTALHFALCGTN-PYMSVKTLIDR 431
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 58-155 1.53e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 53.73  E-value: 1.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921360   58 ENRISEVREILKLDADTVNAKDNDGYTPLHRAAYNNFVDMAKLLLQYHANPNARTELGWTPLH-SACKWNNADCAHLLLQ 136
Cdd:PHA02878 177 ENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHiSVGYCKDYDILKLLLE 256

                         90       100
                 ....*....|....*....|
gi 19921360  137 FGADVNAESDGKQ-TPLHIT 155
Cdd:PHA02878 257 HGVDVNAKSYILGlTALHSS 276
Ank_5 pfam13857
Ankyrin repeats (many copies);
75-122 1.92e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 49.27  E-value: 1.92e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 19921360    75 VNAKDNDGYTPLHRAAYNNFVDMAKLLLQYHANPNARTELGWTPLHSA 122
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
52-102 2.00e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.20  E-value: 2.00e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 19921360    52 ILWAVNENRISEVREILKLDADtVNAKDNDGYTPLHRAAYNNFVDMAKLLL 102
Cdd:pfam13637   5 LHAAAASGHLELLRLLLEKGAD-INAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
34-111 3.79e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 49.34  E-value: 3.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921360    34 ADELIEE--DKNPQSSIERMIL-WAVNENRISEVREILKLDAdtVNAKDNdGYTPLHRAAYNNFVDMAKLLLQYHANPNA 110
Cdd:pfam12796  13 VKLLLENgaDANLQDKNGRTALhLAAKNGHLEIVKLLLEHAD--VNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINV 89


                  .
gi 19921360   111 R 111
Cdd:pfam12796  90 K 90
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 64-156 7.74e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 51.89  E-value: 7.74e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921360   64 VREILKLDADtVNAKDNDGYTPLHRAAYNNFVDMAKLLLQYHANPNARTELGWTPLHSACKWNNADCAHLLLQFGADVNA 143
Cdd:PHA02874 107 IKTILDCGID-VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANV 185

                         90
                 ....*....|...
gi 19921360  144 ESDGKQTPLHITA 156
Cdd:PHA02874 186 KDNNGESPLHNAA 198
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 55-171 1.05e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 51.53  E-value: 1.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921360   55 AVNENRISEVREILKLD--ADTVNAKDndGYTPLHRAAYNNFVDMAKLLLQYHANPNARTELGWTPLHSACKWNNADCAH 132
Cdd:PHA02875  75 AVEEGDVKAVEELLDLGkfADDVFYKD--GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIE 152

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 19921360  133 LLLQFGADVNAESDGKQTPLHITATVSN---CRntatvLLLD 171
Cdd:PHA02875 153 LLIDHKACLDIEDCCGCTPLIIAMAKGDiaiCK-----MLLD 189
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 64-171 1.31e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 51.22  E-value: 1.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921360   64 VREILKLDADtVNAKDNDGYTPLHRAAYNNF-VDMAKLLLQYHANPNARTELGWTPLHSACKWN-NADCAHLLLQFGADV 141
Cdd:PHA02876 290 VPKLLERGAD-VNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANV 368

                         90       100       110
                 ....*....|....*....|....*....|..
gi 19921360  142 NAESDGKQTPLHITATvsncRNTATVL--LLD 171
Cdd:PHA02876 369 NARDYCDKTPIHYAAV----RNNVVIIntLLD 396
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 45-169 2.16e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.67  E-value: 2.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921360   45 QSSIERMIlwAVNEnrisevrEILKLDA--DTVNAKDNDGYTPLHRAAYNNFVDM---------------------AKLL 101
Cdd:PTZ00322  31 PISFERMA--AIQE-------EIARIDThlEALEATENKDATPDHNLTTEEVIDPvvahmltvelcqlaasgdavgARIL 101

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19921360  102 LQYHANPNARTELGWTPLHSACKWNNADCAHLLLQFGADVNA-ESDGKqTPLHItATVSNCRNTATVLL 169
Cdd:PTZ00322 102 LTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLlDKDGK-TPLEL-AEENGFREVVQLLS 168
PHA03095 PHA03095
ankyrin-like protein; Provisional
 64-160 4.12e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 49.64  E-value: 4.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921360   64 VREILKLDADtVNAKDNDGYTPLHRAAYNNFVDMAKL-------------------LLQYHAN----------------- 107
Cdd:PHA03095 135 IRLLLRKGAD-VNALDLYGMTPLAVLLKSRNANVELLrllidagadvyavddrfrsLLHHHLQsfkprarivreliragc 213

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 19921360  108 -PNARTELGWTPLHSACKWNNadCAHLLLQF----GADVNAESDGKQTPLHITATVSN 160
Cdd:PHA03095 214 dPAATDMLGNTPLHSMATGSS--CKRSLVLPlliaGISINARNRYGQTPLHYAAVFNN 269
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 115-143 7.36e-07

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: 44.12  E-value: 7.36e-07
                           10        20
                   ....*....|....*....|....*....
gi 19921360    115 GWTPLHSACKWNNADCAHLLLQFGADVNA 143
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 81-113 7.43e-07

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 44.20  E-value: 7.43e-07
                          10        20        30
                  ....*....|....*....|....*....|....
gi 19921360    81 DGYTPLHRAAY-NNFVDMAKLLLQYHANPNARTE 113
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 59-172 1.16e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 48.12  E-value: 1.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921360   59 NRISEVREILKLDaDTVNAKDNDGYTPLHRAAYNNFVDMAKLLLQYHANPN--ARTELGWTPLHSACKWN---NADCAHL 133
Cdd:PHA03100  13 IKVKNIKYIIMED-DLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINssTKNNSTPLHYLSNIKYNltdVKEIVKL 91

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 19921360  134 LLQFGADVNAESDGKQTPLHITATVSNCRNTATVLLLDR 172
Cdd:PHA03100  92 LLEYGANVNAPDNNGITPLLYAISKKSNSYSIVEYLLDN 130
Ank_4 pfam13637
Ankyrin repeats (many copies);
115-154 2.43e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.42  E-value: 2.43e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 19921360   115 GWTPLHSACKWNNADCAHLLLQFGADVNAESDGKQTPLHI 154
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHF 40
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 115-143 3.25e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 42.66  E-value: 3.25e-06
                          10        20        30
                  ....*....|....*....|....*....|
gi 19921360   115 GWTPLHSAC-KWNNADCAHLLLQFGADVNA 143
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNA 31
PHA03095 PHA03095
ankyrin-like protein; Provisional
 64-172 3.58e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.94  E-value: 3.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921360   64 VREILKLDADtVNAKDNDGYTPLHRAAYNNFV---DMAKLLLQyHANPNARTELGWTPLHSACKWNN-ADCAHLLLQfGA 139
Cdd:PHA03095 205 VRELIRAGCD-PAATDMLGNTPLHSMATGSSCkrsLVLPLLIA-GISINARNRYGQTPLHYAAVFNNpRACRRLIAL-GA 281

                         90       100       110
                 ....*....|....*....|....*....|...
gi 19921360  140 DVNAESDGKQTPLhiTATVSNCRNTATVLLLDR 172
Cdd:PHA03095 282 DINAVSSDGNTPL--SLMVRNNNGRAVRAALAK 312
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 81-110 3.93e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.19  E-value: 3.93e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 19921360     81 DGYTPLHRAAYNNFVDMAKLLLQYHANPNA 110
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 81-110 6.91e-06

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 41.47  E-value: 6.91e-06
                          10        20        30
                  ....*....|....*....|....*....|
gi 19921360    81 DGYTPLHRAAYNNFVDMAKLLLQYHANPNA 110
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 115-143 7.72e-06

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 41.47  E-value: 7.72e-06
                          10        20
                  ....*....|....*....|....*....
gi 19921360   115 GWTPLHSACKWNNADCAHLLLQFGADVNA 143
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 81-171 7.96e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 45.75  E-value: 7.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921360   81 DGYTPLHRAAYNNFVDMAKLLLQYHANPN-----ARTEL-----------------------------GWTPLHSACKWN 126
Cdd:PHA02875  34 DGISPIKLAMKFRDSEAIKLLMKHGAIPDvkypdIESELhdaveegdvkaveelldlgkfaddvfykdGMTPLHLATILK 113

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 19921360  127 NADCAHLLLQFGADVNAESDGKQTPLHITATVSNCRNTAtvLLLD 171
Cdd:PHA02875 114 KLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIE--LLID 156
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 84-174 8.27e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 45.36  E-value: 8.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921360   84 TPLHRAAYNNFVDMAKLLLQYHANPNARTE-LGWTPLHSACKWNNADCAHLLLQFGADVNAESDGKQTPLHITATVsnCR 162
Cdd:PHA02884  72 NPLIYAIDCDNDDAAKLLIRYGADVNRYAEeAKITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELALMI--CN 149

                         90
                 ....*....|..
gi 19921360  163 NTATVLLLDRYI 174
Cdd:PHA02884 150 NFLAFMICDNEI 161
Ank_5 pfam13857
Ankyrin repeats (many copies);
100-154 1.12e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.56  E-value: 1.12e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 19921360   100 LLLQYHANPNARTELGWTPLHSACKWNNADCAHLLLQFGADVNAESDGKQTPLHI 154
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 55-142 1.79e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 44.60  E-value: 1.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921360   55 AVNENRISEVREILKLDADTvNAKDNDGYTPLHRAAYNNFVDMAKLLLQYHANPNARTELGWTPLHSACKWNNADCAHLL 134
Cdd:PHA02875 109 ATILKKLDIMKLLIARGADP-DIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKML 187


                 ....*...
gi 19921360  135 LQFGADVN 142
Cdd:PHA02875 188 LDSGANID 195
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 67-154 3.98e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 43.90  E-value: 3.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921360   67 ILKLDADtVNAKDNDGYTPLHRAAYNNFVDMAKLLLQYHA----------------------------------NPNART 112
Cdd:PHA02876 361 LLELGAN-VNARDYCDKTPIHYAAVRNNVVIINTLLDYGAdiealsqkigtalhfalcgtnpymsvktlidrgaNVNSKN 439

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 19921360  113 ELGWTPLHSACKWN-NADCAHLLLQFGADVNAESDGKQTPLHI 154
Cdd:PHA02876 440 KDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLI 482
PHA02798 PHA02798
ankyrin-like protein; Provisional
 64-183 7.57e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 42.90  E-value: 7.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921360   64 VREILKLDADtVNAKDNDGYTPL-----HRAAYNNFVDMAKLLLQYHANPNARTELGWTPLH---SACKWNNADCAHLLL 135
Cdd:PHA02798  54 VKLFINLGAN-VNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYcllSNGYINNLEILLFMI 132

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 19921360  136 QFGADVNAESDGKQTPLHITATVSNCRNTATV-LLLDRYIQPRKENNSE 183
Cdd:PHA02798 133 ENGADTTLLDKDGFTMLQVYLQSNHHIDIEIIkLLLEKGVDINTHNNKE 181
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 96-169 2.59e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 41.10  E-value: 2.59e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19921360   96 DMAKLLLQYHANPNARTELGWTPLHSACKWNNADCAHLLLQFGADVNAESDGKQTPLHItATVSNCRNTATVLL 169
Cdd:PHA02874 105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHI-AIKHNFFDIIKLLL 177
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 84-197 3.00e-04

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: 41.15  E-value: 3.00e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921360  84 TPLHRAAYNNFVD-MAKLLLQYHANPNARTELGWTPLHSACKWNNADCAHLLLQFGAD-VNAE--SD---GkQTPLHItA 156
Cdd:cd22192  19 SPLLLAAKENDVQaIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPmtSDlyqG-ETALHI-A 96

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 19921360 157 TVSNcrNTATV-LLLDRYiqprkennseelASVI-ARRTGMSF 197
Cdd:cd22192  97 VVNQ--NLNLVrELIARG------------ADVVsPRATGTFF 125
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 35-143 3.35e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 41.22  E-value: 3.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921360    35 DELIEEDKNPQSSIERM----ILWAVNENRISEVREILKLdadtvnaKDNDGY---TPLHrAAYNNFVDMAKLLLQY--- 104
Cdd:TIGR00870  35 RDLEEPKKLNINCPDRLgrsaLFVAAIENENLELTELLLN-------LSCRGAvgdTLLH-AISLEYVDAVEAILLHlla 106

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 19921360   105 ---------HANPNARTEL--GWTPLHSACKWNNADCAHLLLQFGADVNA 143
Cdd:TIGR00870 107 afrksgpleLANDQYTSEFtpGITALHLAAHRQNYEIVKLLLERGASVPA 156
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 32-171 3.36e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 41.20  E-value: 3.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921360   32 DDADELIEEDKNPQSSIERmilwavNENRISEVreILKLDADtVNAKDNDGYTPLHRAAYNNFVDMAKLLLQYHANPNAR 111
Cdd:PHA02876 137 DKINESIEYMKLIKERIQQ------DELLIAEM--LLEGGAD-VNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNII 207

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921360  112 TELGWTPLHSACKWNNADCAHLLLQFGADVNaesdgkQTPLHITATVSNCRNTATVLLLD 171
Cdd:PHA02876 208 ALDDLSVLECAVDSKNIDTIKAIIDNRSNIN------KNDLSLLKAIRNEDLETSLLLYD 261
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 82-160 4.24e-04

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: 40.77  E-value: 4.24e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921360  82 GYTPLHRAAYNNFVDMAKLLLQYHA---NPNA--------RTEL---GWTPLHSACKWNNADCAHLLLQFGADVNAESDG 147
Cdd:cd22192  89 GETALHIAVVNQNLNLVRELIARGAdvvSPRAtgtffrpgPKNLiyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168

                        90
                ....*....|...
gi 19921360 148 KQTPLHITATVSN 160
Cdd:cd22192 169 GNTVLHILVLQPN 181
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 61-139 1.15e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 37.93  E-value: 1.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921360   61 ISEVREILKLDADtVNAKDN-DGYTPLHRAAYNNFVDMAKLLL-QYHANPNARTELGWTPLHSACKWNNADCAHLLLQFG 138
Cdd:PHA02736  71 QEKLKLLMEWGAD-INGKERvFGNTPLHIAVYTQNYELATWLCnQPGVNMEILNYAFKTPYYVACERHDAKMMNILRAKG 149


                 .
gi 19921360  139 A 139
Cdd:PHA02736 150 A 150
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 93-174 1.18e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 39.20  E-value: 1.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921360   93 NFVDMAKLLLQYHANPNARTELGWTPLHSACKWNNADCAHLLLQFGADVNAESDGKQTPLHITATVSNCRNTATVLLLDR 172
Cdd:PHA02875  13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK 92


                 ..
gi 19921360  173 YI 174
Cdd:PHA02875  93 FA 94
PHA02946 PHA02946
ankyin-like protein; Provisional
 76-146 1.60e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 38.88  E-value: 1.60e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19921360   76 NAKDNDGYTPLHRAAYNNFVDMAKLLLQYHANPNARTELGWTPLH--SACKWNNADCAHLLLQFGADVNAESD 146
Cdd:PHA02946  66 NETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYylSGTDDEVIERINLLVQYGAKINNSVD 138
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 16-147 4.01e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 37.93  E-value: 4.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921360   16 LRHAKVPRGMFVsgwDDDADELIEEDKNPqsSIERMILWAVNENRISEVREILK--LDADTVNAKdndGYTPLHRAAYNN 93
Cdd:PLN03192 498 LQHHKELHDLNV---GDLLGDNGGEHDDP--NMASNLLTVASTGNAALLEELLKakLDPDIGDSK---GRTPLHIAASKG 569

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 19921360   94 FVDMAKLLLQYHANPNARTELGWTPLHSACKWNNADCAHLLLQFGADVNAESDG 147
Cdd:PLN03192 570 YEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAG 623
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 43-102 5.22e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 37.54  E-value: 5.22e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921360   43 NPQSSIERMILwAVNENRISEVREILKLDADtVNAKDNDGYTPLHRAAYNNFVDMAKLLL 102
Cdd:PLN03192 618 DPHAAGDLLCT-AAKRNDLTAMKELLKQGLN-VDSEDHQGATALQVAMAEDHVDMVRLLI 675
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 55-120 5.90e-03

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: 37.30  E-value: 5.90e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19921360  55 AVNENrISEVREILKLDADTVNA----------KDNDGY---TPLHRAAYNNFVDMAKLLLQYHANPNARTELGWTPLH 120
Cdd:cd22192  97 VVNQN-LNLVRELIARGADVVSPratgtffrpgPKNLIYygeHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 30-171 6.77e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 36.34  E-value: 6.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921360   30 WDDDADELIEEDKNPqssiermILWAVNENRISEVREILKLDADtvnakDNDGY-TPLHRAAYNNFV--DMAKLLLQYHA 106
Cdd:PHA02859  10 YNDFTDYLFYRYCNP-------LFYYVEKDDIEGVKKWIKFVND-----CNDLYeTPIFSCLEKDKVnvEILKFLIENGA 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19921360  107 NPNARTE-LGWTPLHSACKWN---NADCAHLLLQFGADVNAESDGKQTPLHITATVSNCRNTATVLLLD 171
Cdd:PHA02859  78 DVNFKTRdNNLSALHHYLSFNknvEPEILKILIDSGSSITEEDEDGKNLLHMYMCNFNVRINVIKLLID 146
 
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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