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Conserved domains on  [gi|1002281540|ref|XP_015645069|]
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ankyrin repeat domain-containing protein 2A [Oryza sativa Japonica Group]

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];
21-148 7.79e-28

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 104.27  E-value: 7.79e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281540  21 LIDAARYDDLEDVVALFTAGVSLDSADSQGRTALHMASANGHLAVVQYLIQNGANVNATNSEKNTPLHWACLNGHIEVIK 100
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1002281540 101 ALICAGASVSALNSHEKTPMDEAVTKGKMEVIDAI---GAAVAQAELDGVT 148
Cdd:COG0666   171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLleaGADVNAKDNDGKT 221
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
21-148 7.79e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 104.27  E-value: 7.79e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281540  21 LIDAARYDDLEDVVALFTAGVSLDSADSQGRTALHMASANGHLAVVQYLIQNGANVNATNSEKNTPLHWACLNGHIEVIK 100
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1002281540 101 ALICAGASVSALNSHEKTPMDEAVTKGKMEVIDAI---GAAVAQAELDGVT 148
Cdd:COG0666   171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLleaGADVNAKDNDGKT 221
Ank_2 pfam12796
Ankyrin repeats (3 copies);
21-113 2.55e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.39  E-value: 2.55e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281540  21 LIDAARYDDLEDVVALFTAGVSLDSADSQGRTALHMASANGHLAVVQYLIQNgANVNATNsEKNTPLHWACLNGHIEVIK 100
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1002281540 101 ALICAGASVSALN 113
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 21-115 2.43e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 68.92  E-value: 2.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281540  21 LIDAARYDDLEDVVALF-TAGVSLDSADSQGRTALHMASANGHLAVVQYLIQNGANVNATNSEKNTPLHWACLNGHIEVI 99
Cdd:PHA03100  162 LIDKGVDINAKNRVNYLlSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIF 241

                          90
                  ....*....|....*.
gi 1002281540 100 KALICAGASVSALNSH 115
Cdd:PHA03100  242 KLLLNNGPSIKTIIET 257
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 24-120 2.63e-08

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 51.55  E-value: 2.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281540  24 AARYDDLEDVVALFTAGVSL-----DSADSQGRTALHMASANGHLAVVQYLIQNGANVN---ATN-----SEKNT----- 85
Cdd:cd22192    58 AALYDNLEAAVVLMEAAPELvnepmTSDLYQGETALHIAVVNQNLNLVRELIARGADVVsprATGtffrpGPKNLiyyge 137

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1002281540  86 -PLHWACLNGHIEVIKALICAGASVSALNSHEKTPM 120
Cdd:cd22192   138 hPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 49-78 8.60e-07

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.96  E-value: 8.60e-07
                           10        20        30
                   ....*....|....*....|....*....|
gi 1002281540   49 QGRTALHMASANGHLAVVQYLIQNGANVNA 78
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 21-88 7.63e-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: 35.44  E-value: 7.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281540  21 LIDAARYDDLEDVVALFTAGVSL---------------DSAdSQGRTALHMASANGHLAVVQYLIQNGANVNATNSEKNT 85
Cdd:TIGR00870 132 LHLAAHRQNYEIVKLLLERGASVparacgdffvksqgvDSF-YHGESPLNAAACLGSPSIVALLSEDPADILTADSLGNT 210


                  ...
gi 1002281540  86 PLH 88
Cdd:TIGR00870 211 LLH 213
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
21-148 7.79e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 104.27  E-value: 7.79e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281540  21 LIDAARYDDLEDVVALFTAGVSLDSADSQGRTALHMASANGHLAVVQYLIQNGANVNATNSEKNTPLHWACLNGHIEVIK 100
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1002281540 101 ALICAGASVSALNSHEKTPMDEAVTKGKMEVIDAI---GAAVAQAELDGVT 148
Cdd:COG0666   171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLleaGADVNAKDNDGKT 221
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
21-145 7.03e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 99.26  E-value: 7.03e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281540  21 LIDAARYDDLEDVVALFTAGVSLDSADSQGRTALHMASANGHLAVVQYLIQNGANVNATNSEKNTPLHWACLNGHIEVIK 100
Cdd:COG0666   124 LHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK 203

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1002281540 101 ALICAGASVSALNSHEKTPMDEAVTKGKMEVIDAIGAAVAQAELD 145
Cdd:COG0666   204 LLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAK 248
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
20-148 1.94e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 87.32  E-value: 1.94e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281540  20 DLIDAARYDDLEDVVALFTAGVSLDSADSQGRTALHMASANGHLAVVQYLIQNGANVNATNSEKNTPLHWACLNGHIEVI 99
Cdd:COG0666    57 LLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIV 136

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1002281540 100 KALICAGASVSALNSHEKTPMDEAVTKGKMEVIDAI---GAAVAQAELDGVT 148
Cdd:COG0666   137 KLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLleaGADVNARDNDGET 188
Ank_2 pfam12796
Ankyrin repeats (3 copies);
21-113 2.55e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.39  E-value: 2.55e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281540  21 LIDAARYDDLEDVVALFTAGVSLDSADSQGRTALHMASANGHLAVVQYLIQNgANVNATNsEKNTPLHWACLNGHIEVIK 100
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1002281540 101 ALICAGASVSALN 113
Cdd:pfam12796  79 LLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
21-145 1.34e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 79.61  E-value: 1.34e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281540  21 LIDAARYDDLEDVVALFTAGVSLDSADSQGRTALHMASANGHLAVVQYLIQNGANVNATNSEKNTPLHWACLNGHIEVIK 100
Cdd:COG0666   157 LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVK 236

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1002281540 101 ALICAGASVSALNSHEKTPMDEAVTKGKMEVIDAIGAAVAQAELD 145
Cdd:COG0666   237 LLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAA 281
Ank_4 pfam13637
Ankyrin repeats (many copies);
50-103 3.36e-16

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 68.07  E-value: 3.36e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1002281540  50 GRTALHMASANGHLAVVQYLIQNGANVNATNSEKNTPLHWACLNGHIEVIKALI 103
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
54-135 3.58e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 66.29  E-value: 3.58e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281540  54 LHMASANGHLAVVQYLIQNGANVNATNSEKNTPLHWACLNGHIEVIKALICAGAsvSALNSHEKTPMDEAVTKGKMEVID 133
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78


                  ..
gi 1002281540 134 AI 135
Cdd:pfam12796  79 LL 80
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 21-115 2.43e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 68.92  E-value: 2.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281540  21 LIDAARYDDLEDVVALF-TAGVSLDSADSQGRTALHMASANGHLAVVQYLIQNGANVNATNSEKNTPLHWACLNGHIEVI 99
Cdd:PHA03100  162 LIDKGVDINAKNRVNYLlSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIF 241

                          90
                  ....*....|....*.
gi 1002281540 100 KALICAGASVSALNSH 115
Cdd:PHA03100  242 KLLLNNGPSIKTIIET 257
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 21-125 1.27e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 67.01  E-value: 1.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281540  21 LIDAARYDDLEDVVALFTAGVSLDSADSQGRTALHMASANGHLA-VVQYLIQNGANVNATNSEKNTPLHWACLNGH-IEV 98
Cdd:PHA02876  244 LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTEN 323

                          90       100
                  ....*....|....*....|....*..
gi 1002281540  99 IKALICAGASVSALNSHEKTPMDEAVT 125
Cdd:PHA02876  324 IRTLIMLGADVNAADRLYITPLHQAST 350
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 47-135 9.81e-13

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 64.15  E-value: 9.81e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281540  47 DSQGRTALHMAS-------ANGHLAVVQYLIQNGANVNATNSEKNTPLHWACLNGHIEVIKALICAGASVSALNSHEKTP 119
Cdd:PTZ00322   72 EVIDPVVAHMLTvelcqlaASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTP 151

                          90
                  ....*....|....*.
gi 1002281540 120 MDEAVTKGKMEVIDAI 135
Cdd:PTZ00322  152 LELAEENGFREVVQLL 167
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 36-102 1.91e-12

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 63.38  E-value: 1.91e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002281540  36 LFTAGVSLDSADSQGRTALHMASANGHLAVVQYLIQNGANVNATNSEKNTPLHWACLNGHIEVIKAL 102
Cdd:PTZ00322  101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 36-124 5.94e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 58.91  E-value: 5.94e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281540  36 LFTAGVSLDSADSQGRTALHMASANGH--LAVVQYLIQNGANVNATNSEK----------------NTPLHWACLNGHIE 97
Cdd:PHA03100  127 LLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKNRVNyllsygvpinikdvygFTPLHYAVYNNNPE 206

                          90       100
                  ....*....|....*....|....*..
gi 1002281540  98 VIKALICAGASVSALNSHEKTPMDEAV 124
Cdd:PHA03100  207 FVKYLLDLGANPNLVNKYGDTPLHIAI 233
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
20-148 1.00e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 58.04  E-value: 1.00e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281540  20 DLIDAARYDDLEDVVALFTAGVSLDSADSQGRTALHMASANGHLAVVQYLIQNGANVNATNSEKNTPLHWACLNGHIEVI 99
Cdd:COG0666    24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIV 103

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1002281540 100 KALICAGASVSALNSHEKTPMDEAVTKGKMEVIDAI---GAAVAQAELDGVT 148
Cdd:COG0666   104 KLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLleaGADVNAQDNDGNT 155
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 22-124 1.19e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 58.35  E-value: 1.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281540  22 IDAARYDDLED---VVALFTAGVSLDSAD-SQGRTALHMASANGHLAVVQYLIQNGANVNATNSEKNTPLHWACLNGHIE 97
Cdd:PHA02878  136 IDKKSKDDIIEaeiTKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKP 215

                          90       100
                  ....*....|....*....|....*..
gi 1002281540  98 VIKALICAGASVSALNSHEKTPMDEAV 124
Cdd:PHA02878  216 IVHILLENGASTDARDKCGNTPLHISV 242
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 30-145 2.29e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 57.57  E-value: 2.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281540  30 LEDvvaLFTAGVSLDSADSQGRTALHMASANGHLAVVQYLIQNGANVNATNSEKNTPLHWACLNGH-------------- 95
Cdd:PLN03192  541 LEE---LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHhkifrilyhfasis 617

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281540  96 -----------------IEVIKALICAGASVSALNSHEKTPMDEAVTKGKMEVIDAI---GAAVAQAELD 145
Cdd:PLN03192  618 dphaagdllctaakrndLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLimnGADVDKANTD 687
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 21-80 2.49e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 57.57  E-value: 2.49e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281540  21 LIDAARYDDLEDVVALFTAGVSLDSADSQGRTALHMASANGHLAVVQYLIQNGANVNATN 80
Cdd:PLN03192  626 LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 33-135 2.83e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 57.38  E-value: 2.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281540  33 VVALFTAGVSLDSADSQGRTALHMASANGH-LAVVQYLIQNGANVNATNSEKNTPLHWAC-LNGHIEVIKALICAGASVS 110
Cdd:PHA02876  290 VPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQAStLDRNKDIVITLLELGANVN 369

                          90       100
                  ....*....|....*....|....*
gi 1002281540 111 ALNSHEKTPMDEAVTKGKMEVIDAI 135
Cdd:PHA02876  370 ARDYCDKTPIHYAAVRNNVVIINTL 394
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 36-120 1.11e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 55.45  E-value: 1.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281540  36 LFTAGVSLDSADSQGRTALHMA--SANGHLAVvQYLIQNGANVNATNSEKNTPLHWACLNG-HIEVIKALICAGASVSAL 112
Cdd:PHA02876  394 LLDYGADIEALSQKIGTALHFAlcGTNPYMSV-KTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAI 472


                  ....*...
gi 1002281540 113 NSHEKTPM 120
Cdd:PHA02876  473 NIQNQYPL 480
PHA03095 PHA03095
ankyrin-like protein; Provisional
 26-149 1.19e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 55.42  E-value: 1.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281540  26 RYDDLEDVVALFT-AGVSLDSADSQGRTALH--MASANGHLAVVQYLIQNGANVNATNSEKNTPLHwaCL----NGHIEV 98
Cdd:PHA03095   92 YNATTLDVIKLLIkAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLA--VLlksrNANVEL 169

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1002281540  99 IKALICAGASV--------SALNSHEKTPMDEAvtkGKMEVIDAIGAAVAQAELDGVTV 149
Cdd:PHA03095  170 LRLLIDAGADVyavddrfrSLLHHHLQSFKPRA---RIVRELIRAGCDPAATDMLGNTP 225
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 31-132 1.43e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 54.97  E-value: 1.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281540  31 EDVVALFTAGVSLDSADSQGRTALHMASANGHLAVVQYLIQNGANVNATNSEKNTPLHWACLNGHIEVIKALICAGASVS 110
Cdd:PHA02874  105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184

                          90       100
                  ....*....|....*....|..
gi 1002281540 111 ALNSHEKTPMDEAVTKGKMEVI 132
Cdd:PHA02874  185 VKDNNGESPLHNAAEYGDYACI 206
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 24-148 1.90e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 54.58  E-value: 1.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281540  24 AARYDDLEDVVALFTAGVSLDSADSQGRTALHMASANGHLAVVQYLIQNGANVNATNSEKNTPLHWACLNGHIEVIKALI 103
Cdd:PHA02874  131 AIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLI 210

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1002281540 104 CAGASVSALNSHEKTPMDEAVTKGKMEVIDAI-GAAVAQAELDGVT 148
Cdd:PHA02874  211 DHGNHIMNKCKNGFTPLHNAIIHNRSAIELLInNASINDQDIDGST 256
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 29-113 1.26e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 52.37  E-value: 1.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281540  29 DLEDVVALFTAGVSLDSADSQGRTALHMASA-NGHLAVVQYLIQNGANVNATNSEKNTPLHWACLNGHIEVIKALICAGA 107
Cdd:PHA02876  320 DTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGA 399


                  ....*.
gi 1002281540 108 SVSALN 113
Cdd:PHA02876  400 DIEALS 405
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 22-120 1.46e-08

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 52.22  E-value: 1.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281540  22 IDAARYDDLEDVVALFTAGVSLDSADSQGRTALH--MASANGHLAVVQYLIQNGANVNATNSEKNTPLH----WACL--- 92
Cdd:PHA02716  289 ITLARNIDISVVYSFLQPGVKLHYKDSAGRTCLHqyILRHNISTDIIKLLHEYGNDLNEPDNIGNTVLHtylsMLSVvni 368

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1002281540  93 -------NGHIEVIKALICAGASVSALNSHEKTPM 120
Cdd:PHA02716  369 ldpetdnDIRLDVIQCLISLGADITAVNCLGYTPL 403
PHA03095 PHA03095
ankyrin-like protein; Provisional
 21-119 1.67e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 51.95  E-value: 1.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281540  21 LIDAARYDdLEDVVALFTAGVSLDSADSQGRTALHMASANGH---LAVVQYLIQNGANVNATNSEKNTPLH-WACLNGHI 96
Cdd:PHA03095   19 LLNASNVT-VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTL 97

                          90       100
                  ....*....|....*....|...
gi 1002281540  97 EVIKALICAGASVSALNSHEKTP 119
Cdd:PHA03095   98 DVIKLLIKAGADVNAKDKVGRTP 120
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 24-120 2.63e-08

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 51.55  E-value: 2.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281540  24 AARYDDLEDVVALFTAGVSL-----DSADSQGRTALHMASANGHLAVVQYLIQNGANVN---ATN-----SEKNT----- 85
Cdd:cd22192    58 AALYDNLEAAVVLMEAAPELvnepmTSDLYQGETALHIAVVNQNLNLVRELIARGADVVsprATGtffrpGPKNLiyyge 137

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1002281540  86 -PLHWACLNGHIEVIKALICAGASVSALNSHEKTPM 120
Cdd:cd22192   138 hPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
Ank_5 pfam13857
Ankyrin repeats (many copies);
69-123 3.10e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.34  E-value: 3.10e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1002281540  69 LIQNG-ANVNATNSEKNTPLHWACLNGHIEVIKALICAGASVSALNSHEKTPMDEA 123
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03095 PHA03095
ankyrin-like protein; Provisional
 35-124 4.33e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 50.79  E-value: 4.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281540  35 ALFTAGVSLDSADSQGRTALHMASANGHLA--VVQYLIQNGANVNATNSEKNTPLHWACLNGHIEVIKALICAGASVSAL 112
Cdd:PHA03095  207 ELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAV 286

                          90
                  ....*....|..
gi 1002281540 113 NSHEKTPMDEAV 124
Cdd:PHA03095  287 SSDGNTPLSLMV 298
Ank_4 pfam13637
Ankyrin repeats (many copies);
21-70 5.51e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.50  E-value: 5.51e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1002281540  21 LIDAARYDDLEDVVALFTAGVSLDSADSQGRTALHMASANGHLAVVQYLI 70
Cdd:pfam13637   5 LHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 20-131 6.13e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 50.37  E-value: 6.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281540  20 DLIDAARYDDLEDVVALFTAGVSLDSA-DSQGRTALHMASANGHLAVVQYLIQNGANVNATNSEKNTPLHWACLNGHIEV 98
Cdd:PHA02875   71 ELHDAVEEGDVKAVEELLDLGKFADDVfYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKG 150

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1002281540  99 IKALICAGASVSALNSHEKTPMDEAVTKGKMEV 131
Cdd:PHA02875  151 IELLIDHKACLDIEDCCGCTPLIIAMAKGDIAI 183
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
21-120 6.62e-08

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 49.95  E-value: 6.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281540  21 LIDAARYDDLEDVVALFTAGVSLDSADSQGRTALHMASANGHLAVVQYLIQNGANVNATNSEKNTPLHWACLNGHIEVIK 100
Cdd:COG0666   190 LHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVK 269

                          90       100
                  ....*....|....*....|
gi 1002281540 101 ALICAGASVSALNSHEKTPM 120
Cdd:COG0666   270 LLLLALLLLAAALLDLLTLL 289
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 28-114 1.30e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 49.28  E-value: 1.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281540  28 DDLEDVVALFTAGVSLDSADSQGRTALHMASAN--GHLAVVQYLIQNGANVNATNSEKNTPLHWACLNGHI--EVIKALI 103
Cdd:PHA03100   84 DVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLI 163

                          90
                  ....*....|.
gi 1002281540 104 CAGASVSALNS 114
Cdd:PHA03100  164 DKGVDINAKNR 174
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 31-126 1.70e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 49.11  E-value: 1.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281540  31 EDVV-ALFTAGVSLDSADSQGRTALHMASAN-GHLAVVQYLIQNGANVNATNSEKN-TPLHWACLNGhiEVIKALICAGA 107
Cdd:PHA02878  214 KPIVhILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYILGlTALHSSIKSE--RKLKLLLEYGA 291

                          90
                  ....*....|....*....
gi 1002281540 108 SVSALNSHEKTPMDEAVTK 126
Cdd:PHA02878  292 DINSLNSYKLTPLSSAVKQ 310
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 21-110 2.91e-07

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 48.47  E-value: 2.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281540  21 LIDAARYDDLEDVVALFTAgvslDSAD-----SQGRTALHMASANGHLAVVQYLIQNG---ANVNATNS--EKNTPLHWA 90
Cdd:cd22192    21 LLLAAKENDVQAIKKLLKC----PSCDlfqrgALGETALHVAALYDNLEAAVVLMEAApelVNEPMTSDlyQGETALHIA 96

                          90       100
                  ....*....|....*....|
gi 1002281540  91 CLNGHIEVIKALICAGASVS 110
Cdd:cd22192    97 VVNQNLNLVRELIARGADVV 116
PHA03095 PHA03095
ankyrin-like protein; Provisional
 32-103 5.32e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 47.71  E-value: 5.32e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002281540  32 DVVALFTAGVSLDSADSQGRTALHMASANGHLAVVQYLIQNGANVNATNSEKNTPLHWACLNGHIEVIKALI 103
Cdd:PHA03095  239 LVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 49-80 5.41e-07

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 43.43  E-value: 5.41e-07
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1002281540  49 QGRTALHMASA-NGHLAVVQYLIQNGANVNATN 80
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
PHA03095 PHA03095
ankyrin-like protein; Provisional
 29-148 5.80e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 47.71  E-value: 5.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281540  29 DLEDVVALFTAGVSLDSADSQGRTALH--MASANGHLAVVQYLIQNGANVNATNSEKNTPLHWACLNGHIE--VIKALIC 104
Cdd:PHA03095  166 NVELLRLLIDAGADVYAVDDRFRSLLHhhLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLI 245

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1002281540 105 AGASVSALNSHEKTPMDEAVTKGKMEVID---AIGAAVAQAELDGVT 148
Cdd:PHA03095  246 AGISINARNRYGQTPLHYAAVFNNPRACRrliALGADINAVSSDGNT 292
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 49-78 8.60e-07

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.96  E-value: 8.60e-07
                           10        20        30
                   ....*....|....*....|....*....|
gi 1002281540   49 QGRTALHMASANGHLAVVQYLIQNGANVNA 78
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
41-90 1.22e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.10  E-value: 1.22e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1002281540  41 VSLDSADSQGRTALHMASANGHLAVVQYLIQNGANVNATNSEKNTPLHWA 90
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 33-124 1.25e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 46.58  E-value: 1.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281540  33 VVALFTAGVSLDSADSQGRTALHMASANGH-----LAVVQYLIQNGANVNATNSEKNTPLHWACLN--GHIEVIKALICA 105
Cdd:PHA03100   51 VKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDN 130

                          90
                  ....*....|....*....
gi 1002281540 106 GASVSALNSHEKTPMDEAV 124
Cdd:PHA03100  131 GANVNIKNSDGENLLHLYL 149
Ank_4 pfam13637
Ankyrin repeats (many copies);
84-132 2.25e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.26  E-value: 2.25e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1002281540  84 NTPLHWACLNGHIEVIKALICAGASVSALNSHEKTPMDEAVTKGKMEVI 132
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVL 50
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 50-78 2.74e-06

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 41.86  E-value: 2.74e-06
                          10        20
                  ....*....|....*....|....*....
gi 1002281540  50 GRTALHMASANGHLAVVQYLIQNGANVNA 78
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 65-135 1.01e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 44.10  E-value: 1.01e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002281540  65 VVQYLIQNGANVNATNSEK-NTPLHWACLNGHIEVIKALICAGASVSALNSHEKTPMDEAVTKGKMEVIDAI 135
Cdd:PHA02878  149 ITKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHIL 220
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 82-111 1.12e-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: 39.88  E-value: 1.12e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 1002281540   82 EKNTPLHWACLNGHIEVIKALICAGASVSA 111
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 84-111 2.54e-05

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.16  E-value: 2.54e-05
                          10        20
                  ....*....|....*....|....*...
gi 1002281540  84 NTPLHWACLNGHIEVIKALICAGASVSA 111
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 21-145 3.04e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 42.64  E-value: 3.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281540  21 LIDAARYDDLEDVVALFTAGVSLDSADSQGRTALHMASANGHlAVVQYLIQNgANVNATNSEKNTPLHWA----ClngHI 96
Cdd:PHA02874  194 LHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLINN-ASINDQDIDGSTPLHHAinppC---DI 268

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1002281540  97 EVIKALICAGASVSALNSHEKTPMDEAVTK-GKMEVI-DAIGAAVAQAELD 145
Cdd:PHA02874  269 DIIDILLYHKADISIKDNKGENPIDTAFKYiNKDPVIkDIIANAVLIKEAD 319
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 24-133 6.95e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 41.52  E-value: 6.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281540  24 AARYDDLEDVVALFTAGVSLDSADSQGRTALHMASANGHLAVVQYLIQNGANVNATNSEK-NTPLHWACLNGHIEVIKAL 102
Cdd:PHA02875   42 AMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDgMTPLHLATILKKLDIMKLL 121

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1002281540 103 ICAGASVSALNSHEKTPMDEAVTKGKMEVID 133
Cdd:PHA02875  122 IARGADPDIPNTDKFSPLHLAVMMGDIKGIE 152
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 60-120 7.48e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 40.96  E-value: 7.48e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002281540  60 NGHLAVVQYLIQNGANVNATNSEKN-TPLHWACL---NGHIEVIKALICAGASVSALNSHEKTPM 120
Cdd:PHA02859   63 KVNVEILKFLIENGADVNFKTRDNNlSALHHYLSfnkNVEPEILKILIDSGSSITEEDEDGKNLL 127
PHA02798 PHA02798
ankyrin-like protein; Provisional
 32-113 7.80e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 41.36  E-value: 7.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281540  32 DVVALF-TAGVSLDSADSQGRTAL-----HMASANGHLAVVQYLIQNGANVNATNSEKNTPLHWACLNGHI---EVIKAL 102
Cdd:PHA02798   52 DIVKLFiNLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYInnlEILLFM 131

                          90
                  ....*....|.
gi 1002281540 103 ICAGASVSALN 113
Cdd:PHA02798  132 IENGADTTLLD 142
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 63-135 9.26e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 41.20  E-value: 9.26e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002281540  63 LAVVQYLIQNGANVNATNSEKNTPLHWACLNGHIEVIKALICAGASVSALNSHEKTPMDEAVTKGKMEVIDAI 135
Cdd:PHA02876  158 LLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAI 230
PHA02798 PHA02798
ankyrin-like protein; Provisional
 63-120 2.54e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 39.82  E-value: 2.54e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002281540  63 LAVVQYLIQNGANVNATNSEKNTPLhwaC--------LNGHIEVIKALICAGASVSALNSHEKTPM 120
Cdd:PHA02798   51 TDIVKLFINLGANVNGLDNEYSTPL---CtilsnikdYKHMLDIVKILIENGADINKKNSDGETPL 113
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 28-103 2.56e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 40.05  E-value: 2.56e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002281540  28 DDLEDVVALFTAGVSLDSADSQGRTALHMASANGHLAVVQYLIQNGANVNATNSEKNTPLHWACLNGHIEVIKALI 103
Cdd:PHA02876  156 DELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII 231
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 84-113 2.67e-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: 36.50  E-value: 2.67e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1002281540  84 NTPLHWACL-NGHIEVIKALICAGASVSALN 113
Cdd:pfam00023   3 NTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
PHA03095 PHA03095
ankyrin-like protein; Provisional
 56-120 6.34e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 38.85  E-value: 6.34e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002281540  56 MASANGHLAVVQYLIQNGANVNATNSEKNTPLHwACLNGHI----EVIKALICAGASVSALNSHEKTPM 120
Cdd:PHA03095   20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLH-LYLHYSSekvkDIVRLLLEAGADVNAPERCGFTPL 87
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 65-126 7.21e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 38.49  E-value: 7.21e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002281540  65 VVQYLIQNGANVNATNSEKNTPLHWACLNGHI-----EVIKALICAGASVSALNSHEKTPMDEAVTK 126
Cdd:PHA03100   50 VVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISK 116
PHA02795 PHA02795
ankyrin-like protein; Provisional
 43-96 1.09e-03

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 38.05  E-value: 1.09e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1002281540  43 LDSADSQGRTALHMASANGHLAVVQYLIQNGANVNATNSEKNTPLHWACLNGHI 96
Cdd:PHA02795  214 INQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRGSV 267
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 54-132 1.11e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 38.02  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281540  54 LHMASANGHLAVVQYLIQNGAN-VNATNSEKNTPLHWACLNGHIEVIKALICAGASVSALNSHEKTPMDEAVTKGKMEVI 132
Cdd:PHA02874    5 LRMCIYSGDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDII 84
PHA02946 PHA02946
ankyin-like protein; Provisional
 33-110 1.91e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 37.34  E-value: 1.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281540  33 VVALFTAGVSLDSADSQGRTALHMASANGHLAVVQYLIQNGANVNATNSEKNTPLHWacLNGH----IEVIKALICAGAS 108
Cdd:PHA02946   55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYY--LSGTddevIERINLLVQYGAK 132


                  ..
gi 1002281540 109 VS 110
Cdd:PHA02946  133 IN 134
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 65-115 2.37e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 36.72  E-value: 2.37e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1002281540  65 VVQYLIQNGANVNATNSEKNTPLH-WAC-LNGHIEVIKALICAGASVSALNSH 115
Cdd:PHA02859  105 ILKILIDSGSSITEEDEDGKNLLHmYMCnFNVRINVIKLLIDSGVSFLNKDFD 157
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 47-78 2.49e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all 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.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 37.05  E-value: 2.49e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1002281540  47 DSQGRTALHMASANGHLAVVQYLIQNGANVNA 78
Cdd:cd22194   138 AYEGQTALNIAIERRQGDIVKLLIAKGADVNA 169
PHA02946 PHA02946
ankyin-like protein; Provisional
 66-120 2.79e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 36.96  E-value: 2.79e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1002281540  66 VQYLIQNGANVNATNSEKNTPLHWACLNGHIEVIKALICAGASVSALNSHEKTPM 120
Cdd:PHA02946   55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPL 109
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 49-78 2.84e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). 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.


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 36.76  E-value: 2.84e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1002281540  49 QGRTALHMASANGHLAVVQYLIQNGANVNA 78
Cdd:cd22197    93 RGHSALHIAIEKRSLQCVKLLVENGADVHA 122
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 49-116 3.13e-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: 36.78  E-value: 3.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281540  49 QGRTALHMASANGHLAVVQYLIQNGANVNAT-------NSEKNT------PLHWACLNGHIEVIKALICAGASVSALNSH 115
Cdd:cd21882    72 QGQTALHIAIENRNLNLVRLLVENGADVSARatgrffrKSPGNLfyfgelPLSLAACTNQEEIVRLLLENGAQPAALEAQ 151


                  .
gi 1002281540 116 E 116
Cdd:cd21882   152 D 152
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 54-103 3.50e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 36.40  E-value: 3.50e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1002281540  54 LHMASANGHLAVVQYLIQNGANVNATNSEKNTPLHWACLNGHIEVIKALI 103
Cdd:PHA02878   41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMI 90
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 52-135 7.11e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 35.71  E-value: 7.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281540  52 TALHMASANGHLAVVQYLIQNGANVNATNSEKNTPLHWACLNGHIEVIKALICAGASVSAL------------------- 112
Cdd:PHA02874   37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSILpipciekdmiktildcgid 116

                          90       100
                  ....*....|....*....|....*..
gi 1002281540 113 ----NSHEKTPMDEAVTKGKMEVIDAI 135
Cdd:PHA02874  117 vnikDAELKTFLHYAIKKGDLESIKML 143
PHA02791 PHA02791
ankyrin-like protein; Provisional
 46-132 7.51e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 35.40  E-value: 7.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281540  46 ADSQGRTALHMASANGHLAVVQYLIQNGANVNATNSEknTPLHWACLNGHIEVIKALICAGASVSALNSHEKTPMDEAVT 125
Cdd:PHA02791   26 ADVHGHSALYYAIADNNVRLVCTLLNAGALKNLLENE--FPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVD 103


                  ....*..
gi 1002281540 126 KGKMEVI 132
Cdd:PHA02791  104 SGNMQTV 110
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 21-88 7.63e-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: 35.44  E-value: 7.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281540  21 LIDAARYDDLEDVVALFTAGVSL---------------DSAdSQGRTALHMASANGHLAVVQYLIQNGANVNATNSEKNT 85
Cdd:TIGR00870 132 LHLAAHRQNYEIVKLLLERGASVparacgdffvksqgvDSF-YHGESPLNAAACLGSPSIVALLSEDPADILTADSLGNT 210


                  ...
gi 1002281540  86 PLH 88
Cdd:TIGR00870 211 LLH 213
 
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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