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Conserved domains on  [gi|1622969673|ref|XP_028697801|]
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ankyrin repeat and SOCS box protein 9 isoform X2 [Macaca mulatta]

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
22-261 2.98e-39

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 138.16  E-value: 2.98e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673  22 IRLLSNPLMSDAVSDWSPMHEAAIYGHQLSLRNLISQGWLVNIITADHVSPLHEACLGGHPSCVKILLKHGAQVNGVTTD 101
Cdd:COG0666    40 LLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKD 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673 102 WHTPLFNACVSGSRDCVNLLLQHGASV-QPESDLASPIHEAARRGHAECVDSLIAYGSNIDHKISHLGTPLYLACENQQR 180
Cdd:COG0666   120 GETPLHLAAYNGNLEIVKLLLEAGADVnAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHL 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673 181 ACVKKLLESGADVN-QGKGQDSPLHAVARTASEELACLLMDFGADTQAKNAEGKRPVELVPPDSPLARLFLEREGASLPK 259
Cdd:COG0666   200 EIVKLLLEAGADVNaKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLA 279


                  ..
gi 1622969673 260 PK 261
Cdd:COG0666   280 AA 281
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
22-261 2.98e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 138.16  E-value: 2.98e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673  22 IRLLSNPLMSDAVSDWSPMHEAAIYGHQLSLRNLISQGWLVNIITADHVSPLHEACLGGHPSCVKILLKHGAQVNGVTTD 101
Cdd:COG0666    40 LLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKD 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673 102 WHTPLFNACVSGSRDCVNLLLQHGASV-QPESDLASPIHEAARRGHAECVDSLIAYGSNIDHKISHLGTPLYLACENQQR 180
Cdd:COG0666   120 GETPLHLAAYNGNLEIVKLLLEAGADVnAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHL 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673 181 ACVKKLLESGADVN-QGKGQDSPLHAVARTASEELACLLMDFGADTQAKNAEGKRPVELVPPDSPLARLFLEREGASLPK 259
Cdd:COG0666   200 EIVKLLLEAGADVNaKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLA 279


                  ..
gi 1622969673 260 PK 261
Cdd:COG0666   280 AA 281
Ank_2 pfam12796
Ankyrin repeats (3 copies);
73-163 1.07e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.93  E-value: 1.07e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673  73 LHEACLGGHPSCVKILLKHGAQVNGVTTDWHTPLFNACVSGSRDCVNLLLQHgASVQPESDLASPIHEAARRGHAECVDS 152
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGRTALHYAARSGHLEIVKL 79

                          90
                  ....*....|.
gi 1622969673 153 LIAYGSNIDHK 163
Cdd:pfam12796  80 LLEKGADINVK 90
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 45-236 5.11e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 82.70  E-value: 5.11e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673  45 IYGHQLSL-RNLI-SQGWLVNIITADHVSPLHEACLGGHPSCVKILLKHGAQVNGVTTDWHTPLFNACVSGSRDCVNLLL 122
Cdd:PHA02874    9 IYSGDIEAiEKIIkNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673 123 QHG--ASVQPESDLaspiheaarrgHAECVDSLIAYGSNIDHKISHLGTPLYLACENQQRACVKKLLESGADVN-QGKGQ 199
Cdd:PHA02874   89 DNGvdTSILPIPCI-----------EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNiEDDNG 157

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1622969673 200 DSPLHAVARTASEELACLLMDFGADTQAKNAEGKRPV 236
Cdd:PHA02874  158 CYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPL 194
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 169-227 2.13e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 45.46  E-value: 2.13e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622969673 169 TPLYLACENQQRACVKKLLESGADVN---------QGKGQD------SPLHAVARTASEELACLLMDFGADTQA 227
Cdd:TIGR00870 130 TALHLAAHRQNYEIVKLLLERGASVParacgdffvKSQGVDsfyhgeSPLNAAACLGSPSIVALLSEDPADILT 203
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 68-96 6.88e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.11  E-value: 6.88e-05
                           10        20
                   ....*....|....*....|....*....
gi 1622969673   68 DHVSPLHEACLGGHPSCVKILLKHGAQVN 96
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 73-221 2.08e-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: 39.23  E-value: 2.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673  73 LHEACLGGHPSCVKILLKHGAQ-VN-GVTTDWH---TPLFNACVSGSRDCVNLLLQHGASVQpeSDLASPIheAARRGha 147
Cdd:cd22192    55 LHVAALYDNLEAAVVLMEAAPElVNePMTSDLYqgeTALHIAVVNQNLNLVRELIARGADVV--SPRATGT--FFRPG-- 128

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622969673 148 ecVDSLIAYGsniDHKIShlgtplYLACENQQRAcVKKLLESGADVnqgKGQDS----PLHAVARTASEELACLLMDF 221
Cdd:cd22192   129 --PKNLIYYG---EHPLS------FAACVGNEEI-VRLLIEHGADI---RAQDSlgntVLHILVLQPNKTFACQMYDL 191
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
22-261 2.98e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 138.16  E-value: 2.98e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673  22 IRLLSNPLMSDAVSDWSPMHEAAIYGHQLSLRNLISQGWLVNIITADHVSPLHEACLGGHPSCVKILLKHGAQVNGVTTD 101
Cdd:COG0666    40 LLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKD 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673 102 WHTPLFNACVSGSRDCVNLLLQHGASV-QPESDLASPIHEAARRGHAECVDSLIAYGSNIDHKISHLGTPLYLACENQQR 180
Cdd:COG0666   120 GETPLHLAAYNGNLEIVKLLLEAGADVnAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHL 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673 181 ACVKKLLESGADVN-QGKGQDSPLHAVARTASEELACLLMDFGADTQAKNAEGKRPVELVPPDSPLARLFLEREGASLPK 259
Cdd:COG0666   200 EIVKLLLEAGADVNaKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLA 279


                  ..
gi 1622969673 260 PK 261
Cdd:COG0666   280 AA 281
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
36-234 5.35e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 132.39  E-value: 5.35e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673  36 DWSPMHEAAIYGHQLSLRNLISQGWLVNIITADHVSPLHEACLGGHPSCVKILLKHGAQVNGVTTDWHTPLFNACVSGSR 115
Cdd:COG0666    87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673 116 DCVNLLLQHGASV-QPESDLASPIHEAARRGHAECVDSLIAYGSNIDHKISHLGTPLYLACENQQRACVKKLLESGADVN 194
Cdd:COG0666   167 EIVKLLLEAGADVnARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1622969673 195 -QGKGQDSPLHAVARTASEELACLLMDFGADTQAKNAEGKR 234
Cdd:COG0666   247 aKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
21-238 2.96e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 119.67  E-value: 2.96e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673  21 DIRLLSNPLMSDAVSDWSPMHEAAIYGHQLSLRNLISQGWLVNIITADHVSPLHEACLGGHPSCVKILLKHGAQVNGVTT 100
Cdd:COG0666     6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673 101 DWHTPLFNACVSGSRDCVNLLLQHGASV-QPESDLASPIHEAARRGHAECVDSLIAYGSNIDHKISHLGTPLYLACENQQ 179
Cdd:COG0666    86 GGNTLLHAAARNGDLEIVKLLLEAGADVnARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673 180 RACVKKLLESGADVN-QGKGQDSPLHAVARTASEELACLLMDFGADTQAKNAEGKRPVEL 238
Cdd:COG0666   166 LEIVKLLLEAGADVNaRDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDL 225
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
35-197 9.68e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 113.13  E-value: 9.68e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673  35 SDWSPMHEAAIYGHQLSLRNLISQGWLVNIITADHVSPLHEACLGGHPSCVKILLKHGAQVNGVTTDWHTPLFNACVSGS 114
Cdd:COG0666   119 DGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGH 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673 115 RDCVNLLLQHGASV-QPESDLASPIHEAARRGHAECVDSLIAYGSNIDHKISHLGTPLYLACENQQRACVKKLLESGADV 193
Cdd:COG0666   199 LEIVKLLLEAGADVnAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278


                  ....
gi 1622969673 194 NQGK 197
Cdd:COG0666   279 AAAL 282
Ank_2 pfam12796
Ankyrin repeats (3 copies);
73-163 1.07e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.93  E-value: 1.07e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673  73 LHEACLGGHPSCVKILLKHGAQVNGVTTDWHTPLFNACVSGSRDCVNLLLQHgASVQPESDLASPIHEAARRGHAECVDS 152
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGRTALHYAARSGHLEIVKL 79

                          90
                  ....*....|.
gi 1622969673 153 LIAYGSNIDHK 163
Cdd:pfam12796  80 LLEKGADINVK 90
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 45-236 5.11e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 82.70  E-value: 5.11e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673  45 IYGHQLSL-RNLI-SQGWLVNIITADHVSPLHEACLGGHPSCVKILLKHGAQVNGVTTDWHTPLFNACVSGSRDCVNLLL 122
Cdd:PHA02874    9 IYSGDIEAiEKIIkNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673 123 QHG--ASVQPESDLaspiheaarrgHAECVDSLIAYGSNIDHKISHLGTPLYLACENQQRACVKKLLESGADVN-QGKGQ 199
Cdd:PHA02874   89 DNGvdTSILPIPCI-----------EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNiEDDNG 157

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1622969673 200 DSPLHAVARTASEELACLLMDFGADTQAKNAEGKRPV 236
Cdd:PHA02874  158 CYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPL 194
Ank_2 pfam12796
Ankyrin repeats (3 copies);
40-128 7.32e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 76.31  E-value: 7.32e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673  40 MHEAAIYGHQLSLRNLISQGWLVNIITADHVSPLHEACLGGHPSCVKILLKHgAQVNGVTTDWhTPLFNACVSGSRDCVN 119
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGR-TALHYAARSGHLEIVK 78


                  ....*....
gi 1622969673 120 LLLQHGASV 128
Cdd:pfam12796  79 LLLEKGADI 87
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 85-239 6.54e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 79.54  E-value: 6.54e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673  85 VKILLKHGAQVNGVTTDW-HTPLFNACVSGSRDCVNLLLQHGASVQ-PESDLASPIHEAARRGHAECVDSLIAYGSNIDH 162
Cdd:PHA02878  150 TKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNiPDKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673 163 KISHLGTPLYLA---CENQQraCVKKLLESGADVNQGKG--QDSPLHAVARtaSEELACLLMDFGADTQAKNAEGKRPVE 237
Cdd:PHA02878  230 RDKCGNTPLHISvgyCKDYD--ILKLLLEHGVDVNAKSYilGLTALHSSIK--SERKLKLLLEYGADINSLNSYKLTPLS 305


                  ..
gi 1622969673 238 LV 239
Cdd:PHA02878  306 SA 307
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 38-236 8.12e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 76.64  E-value: 8.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673  38 SPMHEAaIYGHQLS--LRNLISQGWLVNIITADHVSPLHEACLGGHPS-CVKILLKHGAQVNGVTTDWHTPLFNA-CVSG 113
Cdd:PHA02876  275 TPLHHA-SQAPSLSrlVPKLLERGADVNAKNIKGETPLYLMAKNGYDTeNIRTLIMLGADVNAADRLYITPLHQAsTLDR 353

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673 114 SRDCVNLLLQHGASVQPESDL-ASPIHEAARRGHAECVDSLIAYGSNIDHKISHLGTPLYLA-CENQQRACVKKLLESGA 191
Cdd:PHA02876  354 NKDIVITLLELGANVNARDYCdKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGA 433

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1622969673 192 DVN-QGKGQDSPLH-AVARTASEELACLLMDFGADTQAKNAEGKRPV 236
Cdd:PHA02876  434 NVNsKNKDLSTPLHyACKKNCKLDVIEMLLDNGADVNAINIQNQYPL 480
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 17-230 3.17e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 74.70  E-value: 3.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673  17 RDSPDIRLLSNPLMSDaVSDWS---PMHEAAIYGHQLSLRNLISQGWLVNIITADHVSPLHEACLGGH-----PSCVKIL 88
Cdd:PHA03100   14 KVKNIKYIIMEDDLND-YSYKKpvlPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLL 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673  89 LKHGAQVNGVTTDWHTPLFNACV--SGSRDCVNLLLQHGASVQP-ESDLASPIHEAARRGHAEC---------------- 149
Cdd:PHA03100   93 LEYGANVNAPDNNGITPLLYAISkkSNSYSIVEYLLDNGANVNIkNSDGENLLHLYLESNKIDLkilkllidkgvdinak 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673 150 --VDSLIAYGSNIDHKISHLGTPLYLACENQQRACVKKLLESGADVN--QGKGqDSPLHAVARTASEELACLLMDFGADT 225
Cdd:PHA03100  173 nrVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNlvNKYG-DTPLHIAILNNNKEIFKLLLNNGPSI 251


                  ....*
gi 1622969673 226 QAKNA 230
Cdd:PHA03100  252 KTIIE 256
Ank_2 pfam12796
Ankyrin repeats (3 copies);
138-229 1.87e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.06  E-value: 1.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673 138 IHEAARRGHAECVDSLIAYGSNIDHKISHLGTPLYLACENQQRACVKKLLESgADVNQGKGQDSPLHAVARTASEELACL 217
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGRTALHYAARSGHLEIVKL 79

                          90
                  ....*....|..
gi 1622969673 218 LMDFGADTQAKN 229
Cdd:pfam12796  80 LLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 51-239 4.21e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 71.23  E-value: 4.21e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673  51 SLRNLISQGWLVNIITADHVSPLHEACLGGHPSCVKILLKHGAQVNGVTTDWHTPL--FNACVSGSRDCVN---LLLQHG 125
Cdd:PHA03100   17 NIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLhyLSNIKYNLTDVKEivkLLLEYG 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673 126 ASVQPESDLA-SPIHEAA--RRGHAECVDSLIAYGSNIDHKISHLGTPL--YLACENQQRACVKKLLESGADVNQ----- 195
Cdd:PHA03100   97 ANVNAPDNNGiTPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLhlYLESNKIDLKILKLLIDKGVDINAknrvn 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622969673 196 ---GKGQD---------SPLHAVARTASEELACLLMDFGADTQAKNAEGKRPVELV 239
Cdd:PHA03100  177 yllSYGVPinikdvygfTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIA 232
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 43-193 5.99e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 65.27  E-value: 5.99e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673  43 AAIYGHQLSLRNLISQGWLVNIITADHVSPLHEACLGGHPSCVKILLKHGAQVNGVTTDWHTPLFNACVSGSRDCVNLLL 122
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY 611

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622969673 123 QHGASVQPES--DLaspIHEAARRGHAECVDSLIAYGSNIDHKISHLGTPLYLACENQQRACVKKLLESGADV 193
Cdd:PLN03192  612 HFASISDPHAagDL---LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 17-194 7.76e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 64.63  E-value: 7.76e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673  17 RDSPDIRLLsnpLMSDAVSDW------SPMHEAAIYGHQLSLRNLISQGWLVN-IITADHVSPLHEACLGGHPSCVKILL 89
Cdd:PHA02875   46 RDSEAIKLL---MKHGAIPDVkypdieSELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLI 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673  90 KHGAQVNGVTTDWHTPLFNACVSGSRDCVNLLLQHGASVQPESDLA-SPIHEAARRGHAECVDSLIAYGSNIDHkISHLG 168
Cdd:PHA02875  123 ARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGcTPLIIAMAKGDIAICKMLLDSGANIDY-FGKNG 201

                         170       180
                  ....*....|....*....|....*...
gi 1622969673 169 --TPLYLACENQQRACVKKLLESGADVN 194
Cdd:PHA02875  202 cvAALCYAIENNKIDIVRLFIKRGADCN 229
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 37-225 3.19e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 62.70  E-value: 3.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673  37 WSPMHEAAIYGHQLSLRNLISQGWLVNIITADHVSPLHEACLGGHPSCVKILLKHGAQVNGVT-TDWHTPLFNACVSGSR 115
Cdd:PHA02875   36 ISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFyKDGMTPLHLATILKKL 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673 116 DCVNLLLQHGASVQ-PESDLASPIHEAARRGHAECVDSLIAYGSNIDHKISHLGTPLYLACENQQRACVKKLLESGADVN 194
Cdd:PHA02875  116 DIMKLLIARGADPDiPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANID 195

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1622969673 195 Q-GKGQDSPLHAVA-RTASEELACLLMDFGADT 225
Cdd:PHA02875  196 YfGKNGCVAALCYAiENNKIDIVRLFIKRGADC 228
PHA03095 PHA03095
ankyrin-like protein; Provisional
 72-236 1.41e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 60.81  E-value: 1.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673  72 PLHeACLGG---HPSCVKILLKHGAQVNGVTTDWHTPLfnACVSGSRDC----VNLLLQHGASV-QPESDLASPIHEAAR 143
Cdd:PHA03095  120 PLH-VYLSGfniNPKVIRLLLRKGADVNALDLYGMTPL--AVLLKSRNAnvelLRLLIDAGADVyAVDDRFRSLLHHHLQ 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673 144 --RGHAECVDSLIAYGSNIDHKISHLGTPL-YLACENQQRAC-VKKLLESGADVN--QGKGQdSPLHAVARTASEELACL 217
Cdd:PHA03095  197 sfKPRARIVRELIRAGCDPAATDMLGNTPLhSMATGSSCKRSlVLPLLIAGISINarNRYGQ-TPLHYAAVFNNPRACRR 275

                         170
                  ....*....|....*....
gi 1622969673 218 LMDFGADTQAKNAEGKRPV 236
Cdd:PHA03095  276 LIALGADINAVSSDGNTPL 294
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 38-227 5.83e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 59.31  E-value: 5.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673  38 SPMHEAAIYGHQLSLRNLISQGWLVNIITADHVSPLHEACLGGHPSCVK-----------------------------IL 88
Cdd:PHA02876  180 TPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKaiidnrsninkndlsllkairnedletslLL 259

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673  89 LKHGAQVNGVTTDWHTPLFNACVSGS-RDCVNLLLQHGASVQPES-DLASPIHEAARRGH-AECVDSLIAYGSNIDHKIS 165
Cdd:PHA02876  260 YDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNiKGETPLYLMAKNGYdTENIRTLIMLGADVNAADR 339

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622969673 166 HLGTPLYLACE-NQQRACVKKLLESGADVNQGKGQD-SPLHAVARTASEELACLLMDFGADTQA 227
Cdd:PHA02876  340 LYITPLHQASTlDRNKDIVITLLELGANVNARDYCDkTPIHYAAVRNNVVIINTLLDYGADIEA 403
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 55-167 2.24e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 57.37  E-value: 2.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673  55 LISQGWLVNIITADHVSPLHEACLGGHP--SCVKILLKHGAQVN-----------GVTTDW-----HTPLFNACVSGSRD 116
Cdd:PHA03100  127 LLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINaknrvnyllsyGVPINIkdvygFTPLHYAVYNNNPE 206

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1622969673 117 CVNLLLQHGASVQPESDLA-SPIHEAARRGHAECVDSLIAYGSNIDHKISHL 167
Cdd:PHA03100  207 FVKYLLDLGANPNLVNKYGdTPLHIAILNNNKEIFKLLLNNGPSIKTIIETL 258
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 40-252 2.95e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 56.92  E-value: 2.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673  40 MHEAAIYGHQLSLRNLISQGWLVNIITADHVSPLHEACLGGHPSCVKILLKHGAQVNGVTTDWHTPLFNACVSGSRDCVN 119
Cdd:PHA02875    6 LCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673 120 LLLQHGASVQP--ESDLASPIHEAARRGHAECVDSLIAYGSNIDHKISHLGTPLYLACENQQRACVKKLLESGA--DVNQ 195
Cdd:PHA02875   86 ELLDLGKFADDvfYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKAclDIED 165

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622969673 196 GKGQDSPLHAVARtASEELACLLMDFGADTqakNAEGKRP--------VELVPPDspLARLFLER 252
Cdd:PHA02875  166 CCGCTPLIIAMAK-GDIAICKMLLDSGANI---DYFGKNGcvaalcyaIENNKID--IVRLFIKR 224
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 30-183 7.14e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 55.66  E-value: 7.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673  30 MSDAVSDWSPMHEAAIYGHQLSLRNLISQGWLVNIITADHVSPLHEACLGGHPSCVKILLKHGAQVNGVTTDWHTPLFNA 109
Cdd:PHA02878  162 MKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIS 241

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622969673 110 CVS-GSRDCVNLLLQHGASVQPESDLA--SPIHEAARrgHAECVDSLIAYGSNIDHKISHLGTPLYLACenQQRACV 183
Cdd:PHA02878  242 VGYcKDYDILKLLLEHGVDVNAKSYILglTALHSSIK--SERKLKLLLEYGADINSLNSYKLTPLSSAV--KQYLCI 314
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 39-236 2.60e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 54.12  E-value: 2.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673  39 PMHEAAIYGHQLSLRNLISQGWLVNIITADHVSPLHEACLGGHPSCVKILLKHGAQVNgvttdwhtpLFNACVSGSRDCV 118
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCS---------VFYTLVAIKDAFN 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673 119 N--------LLLQHGASVQPESDLASPIHEAARRGHAECVDSLIAYGSNIDHKISHLG-TPLYLACENQQRACVKKLLES 189
Cdd:PHA02878  111 NrnveifkiILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDRHKGnTALHYATENKDQRLTELLLSY 190

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1622969673 190 GADVNQ-GKGQDSPLHAVARTASEELACLLMDFGADTQAKNAEGKRPV 236
Cdd:PHA02878  191 GANVNIpDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPL 238
Ank_2 pfam12796
Ankyrin repeats (3 copies);
37-96 5.86e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 49.34  E-value: 5.86e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673  37 WSPMHEAAIYGHQLSLRNLISQgWLVNIITaDHVSPLHEACLGGHPSCVKILLKHGAQVN 96
Cdd:pfam12796  31 RTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADIN 88
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 42-132 6.82e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.98  E-value: 6.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673  42 EAAIYGHQLSLRNLISQGWLVNIITADHVSPLHEACLGGHPSCVKILLKHGAQVNGVTTDWHTPLFNACVSGSRDCVNLL 121
Cdd:PTZ00322   88 QLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167

                          90
                  ....*....|....*...
gi 1622969673 122 LQH-------GASVQPES 132
Cdd:PTZ00322  168 SRHsqchfelGANAKPDS 185
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 86-239 8.83e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 52.76  E-value: 8.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673  86 KILLKHGAQVNGVTTDWHTPLFNACVSGSRDCVNLLLQHGASVQPES-DLASPIHEAARRGHAECVDSLIAYGSNIDHKi 164
Cdd:PHA02876  162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIAlDDLSVLECAVDSKNIDTIKAIIDNRSNINKN- 240

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622969673 165 shlGTPLYLACENQQRACVKKLLESGADVNQ-GKGQDSPLHAVARTAS-EELACLLMDFGADTQAKNAEGKRPVELV 239
Cdd:PHA02876  241 ---DLSLLKAIRNEDLETSLLLYDAGFSVNSiDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLM 314
Ank_4 pfam13637
Ankyrin repeats (many copies);
37-89 1.61e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.88  E-value: 1.61e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622969673  37 WSPMHEAAIYGHQLSLRNLISQGWLVNIITADHVSPLHEACLGGHPSCVKILL 89
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 55-229 1.75e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 51.60  E-value: 1.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673  55 LISQGWLVNIITADHVSPLHEACLGGHPSCVKILLKHGAQVNGVTTDWHTPLFNACVSGSRDCVNLLLQHGASVQpESDL 134
Cdd:PHA02876  164 LLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNIN-KNDL 242

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673 135 AspIHEAARRGHAECvdSLIAY--GSNIDHKISHLGTPLYLACENQQRA-CVKKLLESGADVNQG--KGQdSPLHAVART 209
Cdd:PHA02876  243 S--LLKAIRNEDLET--SLLLYdaGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKniKGE-TPLYLMAKN 317

                         170       180
                  ....*....|....*....|..
gi 1622969673 210 A--SEELACLLMdFGADTQAKN 229
Cdd:PHA02876  318 GydTENIRTLIM-LGADVNAAD 338
Ank_4 pfam13637
Ankyrin repeats (many copies);
69-122 2.65e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.50  E-value: 2.65e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1622969673  69 HVSPLHEACLGGHPSCVKILLKHGAQVNGVTTDWHTPLFNACVSGSRDCVNLLL 122
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 118-236 4.49e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 50.41  E-value: 4.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673 118 VNLLLQHGASVQPESDLAS-PIHEAARRGHAEC---VDSLIAYGSNIDHKISHLGTPLYLACENQQRACVKKLL-ESGAD 192
Cdd:PHA03095   30 VRRLLAAGADVNFRGEYGKtPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDVIKLLiKAGAD 109

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1622969673 193 VN-QGKGQDSPLHAVARTAS--EELACLLMDFGADTQAKNAEGKRPV 236
Cdd:PHA03095  110 VNaKDKVGRTPLHVYLSGFNinPKVIRLLLRKGADVNALDLYGMTPL 156
PHA03095 PHA03095
ankyrin-like protein; Provisional
 41-257 1.81e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 48.48  E-value: 1.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673  41 HEAAIYGHQLS--------LRNLISQGWLVNIITADHVSPLHEACLGGHPSCVKI---LLKHGAQVNGVTTDWHTPLF-- 107
Cdd:PHA03095   11 MEAALYDYLLNasnvtveeVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHly 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673 108 --NACVsgsRDCVNLLLQHGASVQPESDLA-SPIHEAAR--RGHAECVDSLIAYGSNIDHKISHLGTPL--YLACENQQR 180
Cdd:PHA03095   91 lyNATT---LDVIKLLIKAGADVNAKDKVGrTPLHVYLSgfNINPKVIRLLLRKGADVNALDLYGMTPLavLLKSRNANV 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673 181 ACVKKLLESGADV----NQGkgqDSPLHAVARTASEELACL--LMDFGADTQAKNAEGKRPVELVPPDSPLARL----FL 250
Cdd:PHA03095  168 ELLRLLIDAGADVyavdDRF---RSLLHHHLQSFKPRARIVreLIRAGCDPAATDMLGNTPLHSMATGSSCKRSlvlpLL 244


                  ....*..
gi 1622969673 251 ErEGASL 257
Cdd:PHA03095  245 I-AGISI 250
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 44-129 4.00e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 47.75  E-value: 4.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673  44 AIYGHQ--LSLRNLISQGWLVNIITADHVSPLHEACLGG-HPSCVKILLKHGAQVNGVTTDWHTPLFNACvsGSRDCVNL 120
Cdd:PHA02876  415 ALCGTNpyMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNI 492


                  ....*....
gi 1622969673 121 LLQHGASVQ 129
Cdd:PHA02876  493 LLHYGAELR 501
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 36-128 5.79e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.98  E-value: 5.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673  36 DWSPMHEAAIYGHQLSLRNLISQGWLVNIITADHVSPLHEACLGGHP-SCVKILLKHGAQVNGVTTDWHTPLFNACVSGS 114
Cdd:PHA02876  375 DKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPyMSVKTLIDRGANVNSKNKDLSTPLHYACKKNC 454

                          90
                  ....*....|....*
gi 1622969673 115 R-DCVNLLLQHGASV 128
Cdd:PHA02876  455 KlDVIEMLLDNGADV 469
Ank_4 pfam13637
Ankyrin repeats (many copies);
102-154 6.88e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.65  E-value: 6.88e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622969673 102 WHTPLFNACVSGSRDCVNLLLQHGASV--QPESDLaSPIHEAARRGHAECVDSLI 154
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADInaVDGNGE-TALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
136-187 7.67e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.26  E-value: 7.67e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1622969673 136 SPIHEAARRGHAECVDSLIAYGSNIDHKISHLGTPLYLACENQQRACVKKLL 187
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 169-227 2.13e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 45.46  E-value: 2.13e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622969673 169 TPLYLACENQQRACVKKLLESGADVN---------QGKGQD------SPLHAVARTASEELACLLMDFGADTQA 227
Cdd:TIGR00870 130 TALHLAAHRQNYEIVKLLLERGASVParacgdffvKSQGVDsfyhgeSPLNAAACLGSPSIVALLSEDPADILT 203
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 68-96 6.88e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.11  E-value: 6.88e-05
                           10        20
                   ....*....|....*....|....*....
gi 1622969673   68 DHVSPLHEACLGGHPSCVKILLKHGAQVN 96
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 40-237 2.00e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 42.26  E-value: 2.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673  40 MHEAAIYGHQLSLRNLISQGWLVNIITADHVSPLHEACLGGHPSCVKILLKHGAQVNgvttdwhtplfnacvsgsrdcVN 119
Cdd:PHA02874  128 LHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN---------------------VK 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673 120 lllqhgasvqpESDLASPIHEAARRGHAECVDSLIAYGSNIDHKISHLGTPLYLACENQQRACvkKLLESGADVN-QGKG 198
Cdd:PHA02874  187 -----------DNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAI--ELLINNASINdQDID 253

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1622969673 199 QDSPLH-AVARTASEELACLLMDFGADTQAKNAEGKRPVE 237
Cdd:PHA02874  254 GSTPLHhAINPPCDIDIIDILLYHKADISIKDNKGENPID 293
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 38-128 2.01e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 42.26  E-value: 2.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673  38 SPMHEAAIYGHQLSLRNLISQGWLVNIITADHVSPLHEACLggHPSCVKILLKHGAQVNGVTTDWHTPLFNA----Cvsg 113
Cdd:PHA02874  192 SPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAinppC--- 266

                          90
                  ....*....|....*
gi 1622969673 114 SRDCVNLLLQHGASV 128
Cdd:PHA02874  267 DIDIIDILLYHKADI 281
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 34-121 3.24e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 41.12  E-value: 3.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673  34 VSDWSPMHEAAIYGHQLSLRNLISQGWLVNIITADHV-SPLHEACLGGHPSCVKILLKHGAQVNGVTTDWHTPLFNAcvs 112
Cdd:PHA02884   68 NSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELA--- 144


                  ....*....
gi 1622969673 113 gSRDCVNLL 121
Cdd:PHA02884  145 -LMICNNFL 152
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 104-184 3.68e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 41.12  E-value: 3.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673 104 TPLFNACVSGSRDCVNLLLQHGASVQPESDLA--SPIHEAARRGHAECVDSLIAYGSNIDHKISHLGTPLYLA---CENQ 178
Cdd:PHA02884   72 NPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAkiTPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELAlmiCNNF 151


                  ....*.
gi 1622969673 179 QRACVK 184
Cdd:PHA02884  152 LAFMIC 157
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 169-194 4.88e-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: 4.88e-04
                           10        20
                   ....*....|....*....|....*.
gi 1622969673  169 TPLYLACENQQRACVKKLLESGADVN 194
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADIN 29
PHA03095 PHA03095
ankyrin-like protein; Provisional
 16-122 5.21e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 40.78  E-value: 5.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673  16 PRDSPDI-----RLLSNPLMSDaVSDWSPMHEAAIYG--HQLSLRNLISQGWLVNIITADHVSPLHEA-CLGGHPSCVKi 87
Cdd:PHA03095  198 FKPRARIvreliRAGCDPAATD-MLGNTPLHSMATGSscKRSLVLPLLIAGISINARNRYGQTPLHYAaVFNNPRACRR- 275

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1622969673  88 LLKHGAQVNGVTTDWHTPLFNACVSGSRDCVNLLL 122
Cdd:PHA03095  276 LIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 71-96 1.13e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.73  E-value: 1.13e-03
                          10        20
                  ....*....|....*....|....*..
gi 1622969673  71 SPLHEACL-GGHPSCVKILLKHGAQVN 96
Cdd:pfam00023   4 TPLHLAAGrRGNLEIVKLLLSKGADVN 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 134-260 1.21e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 39.88  E-value: 1.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673 134 LASPIHEAARRGHAECVDSLIAYGSNIDHKISHLGTPLYLACENQQRACVKKLLESGADVN-QGKGQDSPLHAVARTASE 212
Cdd:PTZ00322   82 LTVELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTlLDKDGKTPLELAEENGFR 161

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622969673 213 ELACLLM-------DFGADTQAKNAEGKRPVELVPPDSPLARLFleregASLPKP 260
Cdd:PTZ00322  162 EVVQLLSrhsqchfELGANAKPDSFTGKPPSLEDSPISSHHPDF-----SAVPQP 211
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 68-96 1.72e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 35.31  E-value: 1.72e-03
                          10        20
                  ....*....|....*....|....*....
gi 1622969673  68 DHVSPLHEACLGGHPSCVKILLKHGAQVN 96
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
Ank_5 pfam13857
Ankyrin repeats (many copies);
60-106 1.78e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.79  E-value: 1.78e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1622969673  60 WLVNIITADHVSPLHEACLGGHPSCVKILLKHGAQVNGVTTDWHTPL 106
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 73-221 2.08e-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: 39.23  E-value: 2.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673  73 LHEACLGGHPSCVKILLKHGAQ-VN-GVTTDWH---TPLFNACVSGSRDCVNLLLQHGASVQpeSDLASPIheAARRGha 147
Cdd:cd22192    55 LHVAALYDNLEAAVVLMEAAPElVNePMTSDLYqgeTALHIAVVNQNLNLVRELIARGADVV--SPRATGT--FFRPG-- 128

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622969673 148 ecVDSLIAYGsniDHKIShlgtplYLACENQQRAcVKKLLESGADVnqgKGQDS----PLHAVARTASEELACLLMDF 221
Cdd:cd22192   129 --PKNLIYYG---EHPLS------FAACVGNEEI-VRLLIEHGADI---RAQDSlgntVLHILVLQPNKTFACQMYDL 191
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 101-128 3.36e-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: 34.49  E-value: 3.36e-03
                           10        20
                   ....*....|....*....|....*...
gi 1622969673  101 DWHTPLFNACVSGSRDCVNLLLQHGASV 128
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
PHA02798 PHA02798
ankyrin-like protein; Provisional
 85-195 3.64e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 38.28  E-value: 3.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673  85 VKILLKHGAQVNGVTTDWHTPLfnaCVSGSR--------DCVNLLLQHGASV-QPESDLASPIHEAARRGH---AECVDS 152
Cdd:PHA02798   54 VKLFINLGANVNGLDNEYSTPL---CTILSNikdykhmlDIVKILIENGADInKKNSDGETPLYCLLSNGYinnLEILLF 130

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1622969673 153 LIAYGSNI--DHKISHLGTPLYLACENQ-QRACVKKLLESGADVNQ 195
Cdd:PHA02798  131 MIENGADTtlLDKDGFTMLQVYLQSNHHiDIEIIKLLLEKGVDINT 176
PHA02946 PHA02946
ankyin-like protein; Provisional
 52-211 4.66e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 38.11  E-value: 4.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673  52 LRNLISQGWLVNIITADHVSPLHEACLGGHPSCVKILLKHGAQVNGVTTDWHTPLFNacVSGSRDCV----NLLLQHGAS 127
Cdd:PHA02946   55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYY--LSGTDDEVieriNLLVQYGAK 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673 128 VQPESD---------LASPIHEAARRGHAECVDSLIA--YGSNIDH------------------------KISHLG-TPL 171
Cdd:PHA02946  133 INNSVDeegcgpllaCTDPSERVFKKIMSIGFEARIVdkFGKNHIHrhlmsdnpkastiswmmklgispsKPDHDGnTPL 212

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1622969673 172 YLACENQQRAC-VKKLLESGADVN-QGKGQDSPLHAVARTAS 211
Cdd:PHA02946  213 HIVCSKTVKNVdIINLLLPSTDVNkQNKFGDSPLTLLIKTLS 254
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 102-236 5.79e-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: 37.68  E-value: 5.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673 102 WHTPLFNACVSGSRDCVN-LLLQHGASVQPESDLA-SPIHEAARRGH-------AECVDSLI--AYGSNIdhkisHLG-T 169
Cdd:cd22192    17 SESPLLLAAKENDVQAIKkLLKCPSCDLFQRGALGeTALHVAALYDNleaavvlMEAAPELVnePMTSDL-----YQGeT 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969673 170 PLYLACENQQRACVKKLLESGADVNQG--------KGQDS-------PLHAVARTASEELACLLMDFGADTQAKNAEGKR 234
Cdd:cd22192    92 ALHIAVVNQNLNLVRELIARGADVVSPratgtffrPGPKNliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNT 171


                  ..
gi 1622969673 235 PV 236
Cdd:cd22192   172 VL 173
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 136-161 6.55e-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: 33.33  E-value: 6.55e-03
                           10        20
                   ....*....|....*....|....*.
gi 1622969673  136 SPIHEAARRGHAECVDSLIAYGSNID 161
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADIN 29
Ank_4 pfam13637
Ankyrin repeats (many copies);
169-218 6.90e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 34.17  E-value: 6.90e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1622969673 169 TPLYLACENQQRACVKKLLESGADVN-QGKGQDSPLHAVARTASEELACLL 218
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINaVDGNGETALHFAASNGNVEVLKLL 53
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 169-194 7.76e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 33.38  E-value: 7.76e-03
                          10        20
                  ....*....|....*....|....*.
gi 1622969673 169 TPLYLACENQQRACVKKLLESGADVN 194
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADIN 29
Ank_5 pfam13857
Ankyrin repeats (many copies);
121-174 9.15e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 33.86  E-value: 9.15e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622969673 121 LLQHG--ASVQPESDLASPIHEAARRGHAECVDSLIAYGSNIDHKISHLGTPLYLA 174
Cdd:pfam13857   1 LLEHGpiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
 
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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