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Conserved domains on  [gi|13443014|ref|NP_076992|]
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ankyrin repeat and SOCS box protein 9 isoform 2 [Homo sapiens]

Protein Classification

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

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
22-261 9.04e-40

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 139.32  E-value: 9.04e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014  22 IRLLSNPLMGDAVSDWSPMHEAAIHGHQLSLRNLISQGWAVNIITADHVSPLHEACLGGHLSCVKILLKHGAQVNGVTAD 101
Cdd:COG0666  40 LLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKD 119

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014 102 WHTPLFNACVSGSWDCVNLLLQHGASV-QPESDLASPIHEAARRGHVECVNSLIAYGGNIDHKISHLGTPLYLACENQQR 180
Cdd:COG0666 120 GETPLHLAAYNGNLEIVKLLLEAGADVnAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHL 199

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014 181 ACVKKLLESGADVN-QGKGQDSPLHAVARTASEELACLLMDFGADTQAKNAEGKRPVELVPPESPLAQLFLEREGASLPK 259
Cdd:COG0666 200 EIVKLLLEAGADVNaKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLA 279


                ..
gi 13443014 260 PK 261
Cdd:COG0666 280 AA 281
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
22-261 9.04e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 139.32  E-value: 9.04e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014  22 IRLLSNPLMGDAVSDWSPMHEAAIHGHQLSLRNLISQGWAVNIITADHVSPLHEACLGGHLSCVKILLKHGAQVNGVTAD 101
Cdd:COG0666  40 LLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKD 119

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014 102 WHTPLFNACVSGSWDCVNLLLQHGASV-QPESDLASPIHEAARRGHVECVNSLIAYGGNIDHKISHLGTPLYLACENQQR 180
Cdd:COG0666 120 GETPLHLAAYNGNLEIVKLLLEAGADVnAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHL 199

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014 181 ACVKKLLESGADVN-QGKGQDSPLHAVARTASEELACLLMDFGADTQAKNAEGKRPVELVPPESPLAQLFLEREGASLPK 259
Cdd:COG0666 200 EIVKLLLEAGADVNaKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLA 279


                ..
gi 13443014 260 PK 261
Cdd:COG0666 280 AA 281
Ank_2 pfam12796
Ankyrin repeats (3 copies);
73-163 1.46e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.55  E-value: 1.46e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014    73 LHEACLGGHLSCVKILLKHGAQVNGVTADWHTPLFNACVSGSWDCVNLLLQHgASVQPESDLASPIHEAARRGHVECVNS 152
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGRTALHYAARSGHLEIVKL 79

                          90
                  ....*....|.
gi 13443014   153 LIAYGGNIDHK 163
Cdd:pfam12796  80 LLEKGADINVK 90
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 38-236 1.05e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 79.34  E-value: 1.05e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014   38 SPMHEAaIHGHQLS--LRNLISQGWAVNIITADHVSPLHEACLGGH-LSCVKILLKHGAQVNGVTADWHTPLFNACVSGS 114
Cdd:PHA02876 275 TPLHHA-SQAPSLSrlVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDR 353

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014  115 W-DCVNLLLQHGASVQPESDL-ASPIHEAARRGHVECVNSLIAYGGNIDHKISHLGTPLYLA-CENQQRACVKKLLESGA 191
Cdd:PHA02876 354 NkDIVITLLELGANVNARDYCdKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGA 433

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 13443014  192 DVN-QGKGQDSPLH-AVARTASEELACLLMDFGADTQAKNAEGKRPV 236
Cdd:PHA02876 434 NVNsKNKDLSTPLHyACKKNCKLDVIEMLLDNGADVNAINIQNQYPL 480
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 94-227 1.29e-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: 46.23  E-value: 1.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014    94 QVNGVTADWHTPLFNACVSGS-WDCVNLLLQHGASVQPESDLaspIHeAARRGHVECVNSLIAYGGNIDHKISHLG---- 168
Cdd:TIGR00870  44 NINCPDRLGRSALFVAAIENEnLELTELLLNLSCRGAVGDTL---LH-AISLEYVDAVEAILLHLLAAFRKSGPLEland 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014   169 ----------TPLYLACENQQRACVKKLLESGADVN---------QGKGQD------SPLHAVARTASEELACLLMDFGA 223
Cdd:TIGR00870 120 qytseftpgiTALHLAAHRQNYEIVKLLLERGASVParacgdffvKSQGVDsfyhgeSPLNAAACLGSPSIVALLSEDPA 199


                  ....
gi 13443014   224 DTQA 227
Cdd:TIGR00870 200 DILT 203
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 68-96 4.55e-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: 39.49  E-value: 4.55e-05
                           10        20
                   ....*....|....*....|....*....
gi 13443014     68 DHVSPLHEACLGGHLSCVKILLKHGAQVN 96
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 73-221 2.96e-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: 41.92  E-value: 2.96e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014  73 LHEACLGGHLSCVKILLKHGAQ-VN-GVTADWH---TPLFNACVSGSWDCVNLLLQHGASVQpeSDLASPIHEAARRGhv 147
Cdd:cd22192  55 LHVAALYDNLEAAVVLMEAAPElVNePMTSDLYqgeTALHIAVVNQNLNLVRELIARGADVV--SPRATGTFFRPGPK-- 130

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13443014 148 ecvnSLIAYGgniDHKIShlgtplYLACENQQRAcVKKLLESGADVnqgKGQDS----PLHAVARTASEELACLLMDF 221
Cdd:cd22192 131 ----NLIYYG---EHPLS------FAACVGNEEI-VRLLIEHGADI---RAQDSlgntVLHILVLQPNKTFACQMYDL 191
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
22-261 9.04e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 139.32  E-value: 9.04e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014  22 IRLLSNPLMGDAVSDWSPMHEAAIHGHQLSLRNLISQGWAVNIITADHVSPLHEACLGGHLSCVKILLKHGAQVNGVTAD 101
Cdd:COG0666  40 LLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKD 119

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014 102 WHTPLFNACVSGSWDCVNLLLQHGASV-QPESDLASPIHEAARRGHVECVNSLIAYGGNIDHKISHLGTPLYLACENQQR 180
Cdd:COG0666 120 GETPLHLAAYNGNLEIVKLLLEAGADVnAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHL 199

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014 181 ACVKKLLESGADVN-QGKGQDSPLHAVARTASEELACLLMDFGADTQAKNAEGKRPVELVPPESPLAQLFLEREGASLPK 259
Cdd:COG0666 200 EIVKLLLEAGADVNaKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLA 279


                ..
gi 13443014 260 PK 261
Cdd:COG0666 280 AA 281
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
36-234 1.83e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 133.54  E-value: 1.83e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014  36 DWSPMHEAAIHGHQLSLRNLISQGWAVNIITADHVSPLHEACLGGHLSCVKILLKHGAQVNGVTADWHTPLFNACVSGSW 115
Cdd:COG0666  87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014 116 DCVNLLLQHGASV-QPESDLASPIHEAARRGHVECVNSLIAYGGNIDHKISHLGTPLYLACENQQRACVKKLLESGADVN 194
Cdd:COG0666 167 EIVKLLLEAGADVnARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 13443014 195 -QGKGQDSPLHAVARTASEELACLLMDFGADTQAKNAEGKR 234
Cdd:COG0666 247 aKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
32-238 1.33e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 120.83  E-value: 1.33e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014  32 DAVSDWSPMHEAAIHGHQLSLRNLISQGWAVNIITADHVSPLHEACLGGHLSCVKILLKHGAQVNGVTADWHTPLFNACV 111
Cdd:COG0666  17 LLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAAR 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014 112 SGSWDCVNLLLQHGASV-QPESDLASPIHEAARRGHVECVNSLIAYGGNIDHKISHLGTPLYLACENQQRACVKKLLESG 190
Cdd:COG0666  97 NGDLEIVKLLLEAGADVnARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAG 176

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 13443014 191 ADVN-QGKGQDSPLHAVARTASEELACLLMDFGADTQAKNAEGKRPVEL 238
Cdd:COG0666 177 ADVNaRDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDL 225
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
35-197 2.10e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 115.05  E-value: 2.10e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014  35 SDWSPMHEAAIHGHQLSLRNLISQGWAVNIITADHVSPLHEACLGGHLSCVKILLKHGAQVNGVTADWHTPLFNACVSGS 114
Cdd:COG0666 119 DGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGH 198

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014 115 WDCVNLLLQHGASV-QPESDLASPIHEAARRGHVECVNSLIAYGGNIDHKISHLGTPLYLACENQQRACVKKLLESGADV 193
Cdd:COG0666 199 LEIVKLLLEAGADVnAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278


                ....
gi 13443014 194 NQGK 197
Cdd:COG0666 279 AAAL 282
Ank_2 pfam12796
Ankyrin repeats (3 copies);
73-163 1.46e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.55  E-value: 1.46e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014    73 LHEACLGGHLSCVKILLKHGAQVNGVTADWHTPLFNACVSGSWDCVNLLLQHgASVQPESDLASPIHEAARRGHVECVNS 152
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGRTALHYAARSGHLEIVKL 79

                          90
                  ....*....|.
gi 13443014   153 LIAYGGNIDHK 163
Cdd:pfam12796  80 LLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
40-128 3.56e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.08  E-value: 3.56e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014    40 MHEAAIHGHQLSLRNLISQGWAVNIITADHVSPLHEACLGGHLSCVKILLKHgAQVNGVTADWhTPLFNACVSGSWDCVN 119
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGR-TALHYAARSGHLEIVK 78


                  ....*....
gi 13443014   120 LLLQHGASV 128
Cdd:pfam12796  79 LLLEKGADI 87
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
37-171 1.80e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 80.00  E-value: 1.80e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014  37 WSPMHEAAIHGHQLSLRNLISQGWAVNIITADHVSPLHEACLGGHLSCVKILLKHGAQVNGVTADWHTPLFNACVSGSWD 116
Cdd:COG0666 154 NTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLE 233

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 13443014 117 CVNLLLQHGASVQPE-SDLASPIHEAARRGHVECVNSLIAYGGNIDHKISHLGTPL 171
Cdd:COG0666 234 IVKLLLEAGADLNAKdKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 38-236 1.05e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 79.34  E-value: 1.05e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014   38 SPMHEAaIHGHQLS--LRNLISQGWAVNIITADHVSPLHEACLGGH-LSCVKILLKHGAQVNGVTADWHTPLFNACVSGS 114
Cdd:PHA02876 275 TPLHHA-SQAPSLSrlVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDR 353

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014  115 W-DCVNLLLQHGASVQPESDL-ASPIHEAARRGHVECVNSLIAYGGNIDHKISHLGTPLYLA-CENQQRACVKKLLESGA 191
Cdd:PHA02876 354 NkDIVITLLELGANVNARDYCdKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGA 433

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 13443014  192 DVN-QGKGQDSPLH-AVARTASEELACLLMDFGADTQAKNAEGKRPV 236
Cdd:PHA02876 434 NVNsKNKDLSTPLHyACKKNCKLDVIEMLLDNGADVNAINIQNQYPL 480
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 45-236 1.73e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 78.47  E-value: 1.73e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014   45 IHGHQLSL-RNLI-SQGWAVNIITADHVSPLHEACLGGHLSCVKILLKHGAQVNGVTADWHTPLFNACVSGSWDCVNLLL 122
Cdd:PHA02874   9 IYSGDIEAiEKIIkNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014  123 QHG--ASVQPESDLASpiheaarrghvECVNSLIAYGGNIDHKISHLGTPLYLACENQQRACVKKLLESGADVN-QGKGQ 199
Cdd:PHA02874  89 DNGvdTSILPIPCIEK-----------DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNiEDDNG 157

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 13443014  200 DSPLHAVARTASEELACLLMDFGADTQAKNAEGKRPV 236
Cdd:PHA02874 158 CYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPL 194
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 85-239 2.89e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 78.00  E-value: 2.89e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014   85 VKILLKHGAQVNGVTADW-HTPLFNACVSGSWDCVNLLLQHGASVQ-PESDLASPIHEAARRGHVECVNSLIAYGGNIDH 162
Cdd:PHA02878 150 TKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNiPDKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014  163 KISHLGTPLYLA---CENQQraCVKKLLESGADVNQGKG--QDSPLHAVARtaSEELACLLMDFGADTQAKNAEGKRPVE 237
Cdd:PHA02878 230 RDKCGNTPLHISvgyCKDYD--ILKLLLEHGVDVNAKSYilGLTALHSSIK--SERKLKLLLEYGADINSLNSYKLTPLS 305


                 ..
gi 13443014  238 LV 239
Cdd:PHA02878 306 SA 307
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 17-230 1.63e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 75.47  E-value: 1.63e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014   17 RDFPGIRLLSNPLMGDaVSDWS---PMHEAAIHGHQLSLRNLISQGWAVNIITADHVSPLHEACLGGH-----LSCVKIL 88
Cdd:PHA03100  14 KVKNIKYIIMEDDLND-YSYKKpvlPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLL 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014   89 LKHGAQVNGVTADWHTPLFNACV--SGSWDCVNLLLQHGASVQP-ESDLASPIHEAARRGHVEC---------------- 149
Cdd:PHA03100  93 LEYGANVNAPDNNGITPLLYAISkkSNSYSIVEYLLDNGANVNIkNSDGENLLHLYLESNKIDLkilkllidkgvdinak 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014  150 --VNSLIAYGGNIDHKISHLGTPLYLACENQQRACVKKLLESGADVN--QGKGqDSPLHAVARTASEELACLLMDFGADT 225
Cdd:PHA03100 173 nrVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNlvNKYG-DTPLHIAILNNNKEIFKLLLNNGPSI 251


                 ....*
gi 13443014  226 QAKNA 230
Cdd:PHA03100 252 KTIIE 256
Ank_2 pfam12796
Ankyrin repeats (3 copies);
138-229 2.85e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 66.68  E-value: 2.85e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014   138 IHEAARRGHVECVNSLIAYGGNIDHKISHLGTPLYLACENQQRACVKKLLESgADVNQGKGQDSPLHAVARTASEELACL 217
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGRTALHYAARSGHLEIVKL 79

                          90
                  ....*....|..
gi 13443014   218 LMDFGADTQAKN 229
Cdd:pfam12796  80 LLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 51-237 5.75e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 68.07  E-value: 5.75e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014   51 SLRNLISQGWAVNIITADHVSPLHEACLGGHLSCVKILLKHGAQVNGVTADWHTPLFNACVSGSWDCVNLLLQHGASVQ- 129
Cdd:PHA02874 106 MIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANv 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014  130 PESDLASPIHEAARRGHVECVNSLIAYGGNIDHKISHLGTPLYLACENQQRACvkKLLESGADVN-QGKGQDSPLH-AVA 207
Cdd:PHA02874 186 KDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAI--ELLINNASINdQDIDGSTPLHhAIN 263

                        170       180       190
                 ....*....|....*....|....*....|
gi 13443014  208 RTASEELACLLMDFGADTQAKNAEGKRPVE 237
Cdd:PHA02874 264 PPCDIDIIDILLYHKADISIKDNKGENPID 293
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 43-193 6.94e-13

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 67.97  E-value: 6.94e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014   43 AAIHGHQLSLRNLISQGWAVNIITADHVSPLHEACLGGHLSCVKILLKHGAQVNGVTADWHTPLFNACVSGSWDCVNLLL 122
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY 611

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13443014  123 QHGASVQPES--DLaspIHEAARRGHVECVNSLIAYGGNIDHKISHLGTPLYLACENQQRACVKKLLESGADV 193
Cdd:PLN03192 612 HFASISDPHAagDL---LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 38-194 5.15e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 65.01  E-value: 5.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014   38 SPMHEAAIHGHQLSLRNLISQG-WAVNIITADHVSPLHEACLGGHLSCVKILLKHGAQVNGVTADWHTPLFNACVSGSWD 116
Cdd:PHA02875  70 SELHDAVEEGDVKAVEELLDLGkFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIK 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014  117 CVNLLLQHGASVQPESDLA-SPIHEAARRGHVECVNSLIAYGGNIDHkISHLG--TPLYLACENQQRACVKKLLESGADV 193
Cdd:PHA02875 150 GIELLIDHKACLDIEDCCGcTPLIIAMAKGDIAICKMLLDSGANIDY-FGKNGcvAALCYAIENNKIDIVRLFIKRGADC 228


                 .
gi 13443014  194 N 194
Cdd:PHA02875 229 N 229
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 37-225 2.75e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 63.09  E-value: 2.75e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014   37 WSPMHEAAIHGHQLSLRNLISQGWAVNIITADHVSPLHEACLGGHLSCVKILLKHGAQVNGVT-ADWHTPLFNACVSGSW 115
Cdd:PHA02875  36 ISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFyKDGMTPLHLATILKKL 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014  116 DCVNLLLQHGASVQ-PESDLASPIHEAARRGHVECVNSLIAYGGNIDHKISHLGTPLYLACENQQRACVKKLLESGADVN 194
Cdd:PHA02875 116 DIMKLLIARGADPDiPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANID 195

                        170       180       190
                 ....*....|....*....|....*....|...
gi 13443014  195 Q-GKGQDSPLHAVA-RTASEELACLLMDFGADT 225
Cdd:PHA02875 196 YfGKNGCVAALCYAiENNKIDIVRLFIKRGADC 228
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 55-167 1.61e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 60.83  E-value: 1.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014   55 LISQGWAVNIITADHVSPLHEACLGGH--LSCVKILLKHGAQVN-----------GVTADW-----HTPLFNACVSGSWD 116
Cdd:PHA03100 127 LLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINaknrvnyllsyGVPINIkdvygFTPLHYAVYNNNPE 206

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 13443014  117 CVNLLLQHGASVQPESDLA-SPIHEAARRGHVECVNSLIAYGGNIDHKISHL 167
Cdd:PHA03100 207 FVKYLLDLGANPNLVNKYGdTPLHIAILNNNKEIFKLLLNNGPSIKTIIETL 258
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 30-183 3.06e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 59.89  E-value: 3.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014   30 MGDAVSDWSPMHEAAIHGHQLSLRNLISQGWAVNIITADHVSPLHEACLGGHLSCVKILLKHGAQVNGVTADWHTPLFNA 109
Cdd:PHA02878 162 MKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIS 241

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13443014  110 CVS-GSWDCVNLLLQHGASVQPESDLA--SPIHEAARRGHVecVNSLIAYGGNIDHKISHLGTPLYLACenQQRACV 183
Cdd:PHA02878 242 VGYcKDYDILKLLLEHGVDVNAKSYILglTALHSSIKSERK--LKLLLEYGADINSLNSYKLTPLSSAV--KQYLCI 314
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 40-235 3.48e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 56.54  E-value: 3.48e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014   40 MHEAAIHGHQLSLRNLISQGWAVNIITADHVSPLHEACLGGHLSCVKILLKHGAQVNGVTADWHTPLFNACVSGSWDCVN 119
Cdd:PHA02875   6 LCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014  120 LLLQHGASVQP--ESDLASPIHEAARRGHVECVNSLIAYGGNIDHKISHLGTPLYLACENQQRACVKKLLESGA--DVNQ 195
Cdd:PHA02875  86 ELLDLGKFADDvfYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKAclDIED 165

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 13443014  196 GKGQDSPLHAVARtASEELACLLMDFGADTqakNAEGKRP 235
Cdd:PHA02875 166 CCGCTPLIIAMAK-GDIAICKMLLDSGANI---DYFGKNG 201
Ank_2 pfam12796
Ankyrin repeats (3 copies);
37-96 1.83e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 50.88  E-value: 1.83e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014    37 WSPMHEAAIHGHQLSLRNLISQgWAVNIITaDHVSPLHEACLGGHLSCVKILLKHGAQVN 96
Cdd:pfam12796  31 RTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADIN 88
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 42-132 3.35e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.13  E-value: 3.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014   42 EAAIHGHQLSLRNLISQGWAVNIITADHVSPLHEACLGGHLSCVKILLKHGAQVNGVTADWHTPLFNACVSGSWDCVNLL 121
Cdd:PTZ00322  88 QLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167

                         90
                 ....*....|....*...
gi 13443014  122 LQH-------GASVQPES 132
Cdd:PTZ00322 168 SRHsqchfelGANAKPDS 185
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 38-236 4.53e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.43  E-value: 4.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014   38 SPMHEAAIHGHQLSLRNLISQGWAVNIITADHVSPLHEACLGGHLSCVKILLkhgaqVNGV-TADWHTPLFNAcvsgswD 116
Cdd:PHA02874  37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI-----DNGVdTSILPIPCIEK------D 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014  117 CVNLLLQHGASVQ-PESDLASPIHEAARRGHVECVNSLIAYGGNIDHKISHLGTPLYLACENQQRACVKKLLESGA--DV 193
Cdd:PHA02874 106 MIKTILDCGIDVNiKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAyaNV 185

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 13443014  194 NQGKGqDSPLHAVARTASEELACLLMDFGADTQAKNAEGKRPV 236
Cdd:PHA02874 186 KDNNG-ESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPL 227
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 55-229 4.88e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 53.53  E-value: 4.88e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014   55 LISQGWAVNIITADHVSPLHEACLGGHLSCVKILLKHGAQVNGVTADWHTPLFNACVSGSWDCVNLLLQHGASVQpESDL 134
Cdd:PHA02876 164 LLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNIN-KNDL 242

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014  135 AspIHEAARRGHVEcvNSLIAY--GGNIDHKISHLGTPLYLACENQQRA-CVKKLLESGADVNQG--KGQdSPLHAVART 209
Cdd:PHA02876 243 S--LLKAIRNEDLE--TSLLLYdaGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKniKGE-TPLYLMAKN 317

                        170       180
                 ....*....|....*....|..
gi 13443014  210 A--SEELACLLMdFGADTQAKN 229
Cdd:PHA02876 318 GydTENIRTLIM-LGADVNAAD 338
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 52-209 5.32e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 53.35  E-value: 5.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014   52 LRNLISQGWAVNIITADHV-SPLHEACLGGHLSCVKILLKHGAQVNGVTADWHTPLFNACVSGSWDCVNLLLQHGASVQP 130
Cdd:PHA02878 150 TKLLLSYGADINMKDRHKGnTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014  131 ESDLA-SPIHEAARR-GHVECVNSLIAYGGNIDHKISHLG-TPLYLACENQQRacVKKLLESGADVNQ-GKGQDSPLHAV 206
Cdd:PHA02878 230 RDKCGnTPLHISVGYcKDYDILKLLLEHGVDVNAKSYILGlTALHSSIKSERK--LKLLLEYGADINSlNSYKLTPLSSA 307


                 ...
gi 13443014  207 ART 209
Cdd:PHA02878 308 VKQ 310
PHA03095 PHA03095
ankyrin-like protein; Provisional
 72-236 5.96e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 53.10  E-value: 5.96e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014   72 PLHeACLGG---HLSCVKILLKHGAQVNGVTADWHTPLF------NACVsgswDCVNLLLQHGASV-QPESDLASPIHEA 141
Cdd:PHA03095 120 PLH-VYLSGfniNPKVIRLLLRKGADVNALDLYGMTPLAvllksrNANV----ELLRLLIDAGADVyAVDDRFRSLLHHH 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014  142 AR--RGHVECVNSLIAYGGNIDHKISHLGTPL-YLACENQQRAC-VKKLLESGADVN--QGKGQdSPLHAVARTASEELA 215
Cdd:PHA03095 195 LQsfKPRARIVRELIRAGCDPAATDMLGNTPLhSMATGSSCKRSlVLPLLIAGISINarNRYGQ-TPLHYAAVFNNPRAC 273

                        170       180
                 ....*....|....*....|.
gi 13443014  216 CLLMDFGADTQAKNAEGKRPV 236
Cdd:PHA03095 274 RRLIALGADINAVSSDGNTPL 294
Ank_4 pfam13637
Ankyrin repeats (many copies);
37-89 6.58e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.04  E-value: 6.58e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 13443014    37 WSPMHEAAIHGHQLSLRNLISQGWAVNIITADHVSPLHEACLGGHLSCVKILL 89
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 82-239 1.17e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 52.37  E-value: 1.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014   82 LSCVKILLKHGAQVNGVTADWHTPLFNACVSGSWDCVNLLLQHGASVQPES-DLASPIHEAARRGHVECVNSLIAYGGNI 160
Cdd:PHA02876 158 LLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIAlDDLSVLECAVDSKNIDTIKAIIDNRSNI 237

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014  161 DHKishlGTPLYLACENQQRACVKKLLESGADVNQ-GKGQDSPLHAVARTAS-EELACLLMDFGADTQAKNAEGKRPVEL 238
Cdd:PHA02876 238 NKN----DLSLLKAIRNEDLETSLLLYDAGFSVNSiDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYL 313


                 .
gi 13443014  239 V 239
Cdd:PHA02876 314 M 314
PHA03095 PHA03095
ankyrin-like protein; Provisional
 147-235 1.18e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 51.95  E-value: 1.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014  147 VECVNSLIAYGGNIDHKISHLGTPL--YLACENQQRA-CVKKLLESGADVN-QGKGQDSPLHAVARTASEE-LACLLMDF 221
Cdd:PHA03095  27 VEEVRRLLAAGADVNFRGEYGKTPLhlYLHYSSEKVKdIVRLLLEAGADVNaPERCGFTPLHLYLYNATTLdVIKLLIKA 106

                         90
                 ....*....|....
gi 13443014  222 GADTQAKNAEGKRP 235
Cdd:PHA03095 107 GADVNAKDKVGRTP 120
Ank_4 pfam13637
Ankyrin repeats (many copies);
69-122 1.42e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.27  E-value: 1.42e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 13443014    69 HVSPLHEACLGGHLSCVKILLKHGAQVNGVTADWHTPLFNACVSGSWDCVNLLL 122
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 118-236 4.10e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 50.41  E-value: 4.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014  118 VNLLLQHGASVQPESDLAS-PIHEAARRGHVEC---VNSLIAYGGNIDHKISHLGTPLYLACENQQRACVKKLL-ESGAD 192
Cdd:PHA03095  30 VRRLLAAGADVNFRGEYGKtPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDVIKLLiKAGAD 109

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 13443014  193 VN-QGKGQDSPLHAVARTAS--EELACLLMDFGADTQAKNAEGKRPV 236
Cdd:PHA03095 110 VNaKDKVGRTPLHVYLSGFNinPKVIRLLLRKGADVNALDLYGMTPL 156
PHA03095 PHA03095
ankyrin-like protein; Provisional
 52-235 3.84e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 47.33  E-value: 3.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014   52 LRNLISQGWAVNIITADHVSPLHeACLggHLSC------VKILLKHGAQVNGVTADWHTPLF----NACVsgsWDCVNLL 121
Cdd:PHA03095  30 VRRLLAAGADVNFRGEYGKTPLH-LYL--HYSSekvkdiVRLLLEAGADVNAPERCGFTPLHlylyNATT---LDVIKLL 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014  122 LQHGASVQPESDLA-SPIHEAAR--RGHVECVNSLIAYGGNIDHKISHLGTPL--YLACENQQRACVKKLLESGADV--- 193
Cdd:PHA03095 104 IKAGADVNAKDKVGrTPLHVYLSgfNINPKVIRLLLRKGADVNALDLYGMTPLavLLKSRNANVELLRLLIDAGADVyav 183

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 13443014  194 -NQGkgqDSPLHAVARTASEELACL--LMDFGADTQAKNAEGKRP 235
Cdd:PHA03095 184 dDRF---RSLLHHHLQSFKPRARIVreLIRAGCDPAATDMLGNTP 225
Ank_4 pfam13637
Ankyrin repeats (many copies);
102-154 4.58e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.03  E-value: 4.58e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 13443014   102 WHTPLFNACVSGSWDCVNLLLQHGASV--QPESDLaSPIHEAARRGHVECVNSLI 154
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADInaVDGNGE-TALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
136-187 5.75e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.65  E-value: 5.75e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 13443014   136 SPIHEAARRGHVECVNSLIAYGGNIDHKISHLGTPLYLACENQQRACVKKLL 187
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 94-227 1.29e-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: 46.23  E-value: 1.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014    94 QVNGVTADWHTPLFNACVSGS-WDCVNLLLQHGASVQPESDLaspIHeAARRGHVECVNSLIAYGGNIDHKISHLG---- 168
Cdd:TIGR00870  44 NINCPDRLGRSALFVAAIENEnLELTELLLNLSCRGAVGDTL---LH-AISLEYVDAVEAILLHLLAAFRKSGPLEland 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014   169 ----------TPLYLACENQQRACVKKLLESGADVN---------QGKGQD------SPLHAVARTASEELACLLMDFGA 223
Cdd:TIGR00870 120 qytseftpgiTALHLAAHRQNYEIVKLLLERGASVParacgdffvKSQGVDsfyhgeSPLNAAACLGSPSIVALLSEDPA 199


                  ....
gi 13443014   224 DTQA 227
Cdd:TIGR00870 200 DILT 203
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 106-238 1.50e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 45.75  E-value: 1.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014  106 LFNACVSGSWDCVNLLLQHGasVQPESDLA---SPIHEAARRGHVECVNSLIAYGGNIDHKISHLGTPLYLACENQQRAC 182
Cdd:PHA02875   6 LCDAILFGELDIARRLLDIG--INPNFEIYdgiSPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKA 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 13443014  183 VKKLLESGA---DVNQGKGqDSPLHAVARTASEELACLLMDFGADTQAKNAEGKRPVEL 238
Cdd:PHA02875  84 VEELLDLGKfadDVFYKDG-MTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHL 141
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 40-141 2.95e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 44.57  E-value: 2.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014   40 MHEAAIHGHQLSLRNLISQGWAVNIITADHVSPLHEACLGGHLSCVKILLKHGAQVNGVTADWHTPLFNACVSGSWDCVN 119
Cdd:PHA02874 128 LHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIK 207

                         90       100
                 ....*....|....*....|...
gi 13443014  120 LLLQHGASVQPESDLA-SPIHEA 141
Cdd:PHA02874 208 LLIDHGNHIMNKCKNGfTPLHNA 230
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 50-129 3.12e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.05  E-value: 3.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014   50 LSLRNLISQGWAVNIITADHVSPLHEACLGG-HLSCVKILLKHGAQVNGVTADWHTPLFNACvsGSWDCVNLLLQHGASV 128
Cdd:PHA02876 423 MSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLHYGAEL 500


                 .
gi 13443014  129 Q 129
Cdd:PHA02876 501 R 501
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 68-96 4.55e-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: 39.49  E-value: 4.55e-05
                           10        20
                   ....*....|....*....|....*....
gi 13443014     68 DHVSPLHEACLGGHLSCVKILLKHGAQVN 96
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 36-128 1.07e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 43.13  E-value: 1.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014   36 DWSPMHEAAIHGHQLSLRNLISQGWAVNIITADHVSPLHEACLGGH-LSCVKILLKHGAQVNGVTADWHTPLFNACVSG- 113
Cdd:PHA02876 375 DKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNpYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNc 454

                         90
                 ....*....|....*
gi 13443014  114 SWDCVNLLLQHGASV 128
Cdd:PHA02876 455 KLDVIEMLLDNGADV 469
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 104-184 2.93e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 41.51  E-value: 2.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014  104 TPLFNACVSGSWDCVNLLLQHGASVQPESDLA--SPIHEAARRGHVECVNSLIAYGGNIDHKISHLGTPLYLA---CENQ 178
Cdd:PHA02884  72 NPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAkiTPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELAlmiCNNF 151


                 ....*.
gi 13443014  179 QRACVK 184
Cdd:PHA02884 152 LAFMIC 157
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 73-221 2.96e-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: 41.92  E-value: 2.96e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014  73 LHEACLGGHLSCVKILLKHGAQ-VN-GVTADWH---TPLFNACVSGSWDCVNLLLQHGASVQpeSDLASPIHEAARRGhv 147
Cdd:cd22192  55 LHVAALYDNLEAAVVLMEAAPElVNePMTSDLYqgeTALHIAVVNQNLNLVRELIARGADVV--SPRATGTFFRPGPK-- 130

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13443014 148 ecvnSLIAYGgniDHKIShlgtplYLACENQQRAcVKKLLESGADVnqgKGQDS----PLHAVARTASEELACLLMDF 221
Cdd:cd22192 131 ----NLIYYG---EHPLS------FAACVGNEEI-VRLLIEHGADI---RAQDSlgntVLHILVLQPNKTFACQMYDL 191
PHA03095 PHA03095
ankyrin-like protein; Provisional
 22-158 3.38e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 41.55  E-value: 3.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014   22 IRLLSNPLMGDaVSDWSPMHEAAIHG--HQLSLRNLISQGWAVNIITADHVSPLHEA-CLGGHLSCVKiLLKHGAQVNGV 98
Cdd:PHA03095 209 IRAGCDPAATD-MLGNTPLHSMATGSscKRSLVLPLLIAGISINARNRYGQTPLHYAaVFNNPRACRR-LIALGADINAV 286

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13443014   99 TADWHTPLFNACVSGSWDCVNLLLqhgaSVQPESDL-ASPIHEAARRGHV-------ECVNSLIAYGG 158
Cdd:PHA03095 287 SSDGNTPLSLMVRNNNGRAVRAAL----AKNPSAETvAATLNTASVAGGDipsdatrLCVAKVVLRGA 350
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 169-194 5.44e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.41  E-value: 5.44e-04
                           10        20
                   ....*....|....*....|....*.
gi 13443014    169 TPLYLACENQQRACVKKLLESGADVN 194
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 39-141 5.98e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 40.72  E-value: 5.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014   39 PMHEAAIHGHQLSLRNLISQGWAVNIITADHVSPLHEACLGGHLSCVKILLKHGAQVNGVTADWHTPLFNACVSGSwDCV 118
Cdd:PHA02874 160 PIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAI 238

                         90       100
                 ....*....|....*....|...
gi 13443014  119 NLLLQHGASVQPESDLASPIHEA 141
Cdd:PHA02874 239 ELLINNASINDQDIDGSTPLHHA 261
Ank_5 pfam13857
Ankyrin repeats (many copies);
60-106 7.61e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.94  E-value: 7.61e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 13443014    60 WAVNIITADHVSPLHEACLGGHLSCVKILLKHGAQVNGVTADWHTPL 106
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PHA02946 PHA02946
ankyin-like protein; Provisional
 52-239 7.64e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 40.42  E-value: 7.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014   52 LRNLISQGWAVNIITADHVSPLHEACLGGHLSCVKILLKHGAQVNGVTADWHTPLFNacVSGSWDCVnlllqhgasvqpe 131
Cdd:PHA02946  55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYY--LSGTDDEV------------- 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014  132 sdlaspiheaarrghVECVNSLIAYGGNIDHKISHLGTPLYLACENQQRACVKKLLESGAD---VNQGKGQDSPLHAVAR 208
Cdd:PHA02946 120 ---------------IERINLLVQYGAKINNSVDEEGCGPLLACTDPSERVFKKIMSIGFEariVDKFGKNHIHRHLMSD 184

                        170       180       190
                 ....*....|....*....|....*....|.
gi 13443014  209 TASEELACLLMDFGADTQAKNAEGKRPVELV 239
Cdd:PHA02946 185 NPKASTISWMMKLGISPSKPDHDGNTPLHIV 215
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 71-96 8.27e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.11  E-value: 8.27e-04
                          10        20
                  ....*....|....*....|....*..
gi 13443014    71 SPLHEACL-GGHLSCVKILLKHGAQVN 96
Cdd:pfam00023   4 TPLHLAAGrRGNLEIVKLLLSKGADVN 30
PHA02798 PHA02798
ankyrin-like protein; Provisional
 85-195 1.18e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 39.82  E-value: 1.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014   85 VKILLKHGAQVNGVTADWHTPLfnaCV--------SGSWDCVNLLLQHGASV-QPESDLASPIHEAARRGHV---ECVNS 152
Cdd:PHA02798  54 VKLFINLGANVNGLDNEYSTPL---CTilsnikdyKHMLDIVKILIENGADInKKNSDGETPLYCLLSNGYInnlEILLF 130

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 13443014  153 LIAYGGNI--DHKISHLGTPLYLACENQ-QRACVKKLLESGADVNQ 195
Cdd:PHA02798 131 MIENGADTtlLDKDGFTMLQVYLQSNHHiDIEIIKLLLEKGVDINT 176
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 153-260 1.22e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 39.88  E-value: 1.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014  153 LIAYGGNIDHKISHLGTPLYLACENQQRACVKKLLESGADVN-QGKGQDSPLHAVARTASEELACLLM-------DFGAD 224
Cdd:PTZ00322 101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTlLDKDGKTPLELAEENGFREVVQLLSrhsqchfELGAN 180

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 13443014  225 TQAKNAEGKRPVELVPPESPLAQLFleregASLPKP 260
Cdd:PTZ00322 181 AKPDSFTGKPPSLEDSPISSHHPDF-----SAVPQP 211
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 102-236 1.29e-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: 40.00  E-value: 1.29e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014 102 WHTPLFNACVSGSWDCVN-LLLQHGASVQPESDLA-SPIHEAARRGHVECVNSLI-AYGGNIDHKIS---HLG-TPLYLA 174
Cdd:cd22192  17 SESPLLLAAKENDVQAIKkLLKCPSCDLFQRGALGeTALHVAALYDNLEAAVVLMeAAPELVNEPMTsdlYQGeTALHIA 96

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13443014 175 CENQQRACVKKLLESGADVNQG--------KGQDS-------PLHAVARTASEELACLLMDFGADTQAKNAEGKRPV 236
Cdd:cd22192  97 VVNQNLNLVRELIARGADVVSPratgtffrPGPKNliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 78-231 2.04e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 39.09  E-value: 2.04e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014  78 LGGHLSCVKILLKHGAQVNGVTADwhTPLFNACV---SGSWDCVNLLLQhgasVQPESDLASPIHEAarrghvECVNSLi 154
Cdd:cd21882   4 LLGLLECLRWYLTDSAYQRGATGK--TCLHKAALnlnDGVNEAIMLLLE----AAPDSGNPKELVNA------PCTDEF- 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014 155 aYGGNidhkishlgTPLYLACENQQRACVKKLLESGADV-----------NQGKG---QDSPLHAVARTASEELACLLMD 220
Cdd:cd21882  71 -YQGQ---------TALHIAIENRNLNLVRLLVENGADVsaratgrffrkSPGNLfyfGELPLSLAACTNQEEIVRLLLE 140

                       170
                ....*....|.
gi 13443014 221 FGADTQAKNAE 231
Cdd:cd21882 141 NGAQPAALEAQ 151
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 136-161 2.31e-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: 34.87  E-value: 2.31e-03
                           10        20
                   ....*....|....*....|....*.
gi 13443014    136 SPIHEAARRGHVECVNSLIAYGGNID 161
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADIN 29
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 68-96 2.84e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.54  E-value: 2.84e-03
                          10        20
                  ....*....|....*....|....*....
gi 13443014    68 DHVSPLHEACLGGHLSCVKILLKHGAQVN 96
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 183-238 3.11e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 38.73  E-value: 3.11e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 13443014  183 VKKLLESGADVN-QGKGQDSPLHAVARTASEELACLLMDFGADTQAKNAEGKRPVEL 238
Cdd:PTZ00322  98 ARILLTGGADPNcRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLEL 154
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 160-235 3.40e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 38.49  E-value: 3.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014  160 IDHKISHLGTPLYLACENQQRACVKKLLESGADVNQ-GKGQDSPLHAVAR-----TASEELACLLMDFGADTQAKNAEGK 233
Cdd:PHA03100  28 NDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSsTKNNSTPLHYLSNikynlTDVKEIVKLLLEYGANVNAPDNNGI 107


                 ..
gi 13443014  234 RP 235
Cdd:PHA03100 108 TP 109
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 38-128 3.66e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 38.41  E-value: 3.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13443014   38 SPMHEAAIHGHQLSLRNLISQGWAVNIITADHVSPLHEACLggHLSCVKILLKHGAQVNGVTADWHTPLFNA----Cvsg 113
Cdd:PHA02874 192 SPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAinppC--- 266

                         90
                 ....*....|....*
gi 13443014  114 SWDCVNLLLQHGASV 128
Cdd:PHA02874 267 DIDIIDILLYHKADI 281
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 34-106 4.32e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 37.66  E-value: 4.32e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13443014   34 VSDWSPMHEAAIHGHQLSLRNLISQGWAVNIITADHV-SPLHEACLGGHLSCVKILLKHGAQVNGVTADWHTPL 106
Cdd:PHA02884  68 NSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPI 141
PHA03095 PHA03095
ankyrin-like protein; Provisional
 171-238 4.75e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 38.08  E-value: 4.75e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13443014  171 LYLACENQQRAC---VKKLLESGADVNQGKGQDS-PLHAVARTASEELA---CLLMDFGADTQAKNAEGKRPVEL 238
Cdd:PHA03095  15 LYDYLLNASNVTveeVRRLLAAGADVNFRGEYGKtPLHLYLHYSSEKVKdivRLLLEAGADVNAPERCGFTPLHL 89
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 66-129 6.18e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 37.75  E-value: 6.18e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13443014    66 TADHvSPLHEACLGGHLSCVKILLKHGAQVN------------GVTADWHT--PL-FNACVsGSWDCVNLLLQHGASVQ 129
Cdd:TIGR00870 126 TPGI-TALHLAAHRQNYEIVKLLLERGASVParacgdffvksqGVDSFYHGesPLnAAACL-GSPSIVALLSEDPADIL 202
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 101-128 6.95e-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: 6.95e-03
                           10        20
                   ....*....|....*....|....*...
gi 13443014    101 DWHTPLFNACVSGSWDCVNLLLQHGASV 128
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
Ank_4 pfam13637
Ankyrin repeats (many copies);
169-218 9.01e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 33.79  E-value: 9.01e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 13443014   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 9.45e-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: 33.00  E-value: 9.45e-03
                          10        20
                  ....*....|....*....|....*.
gi 13443014   169 TPLYLACENQQRACVKKLLESGADVN 194
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADIN 29
 
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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