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Conserved domains on  [gi|34782874|gb|AAH07020|]
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ANKRD7 protein, partial [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];
1-116 6.03e-32

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 115.44  E-value: 6.03e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782874   1 AVQCQNEDCATILLNFGADPDLRDIRYNTVLHYAVCGQSLSLVEKLLEYEADLEAKNKDGYTPLLVAVINNNPKMVKFLL 80
Cdd:COG0666  94 AARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLL 173

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 34782874  81 EKGADVNASDNYQRTALILAVSGEPPCLVKLLLQQG 116
Cdd:COG0666 174 EAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAG 209
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-116 6.03e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 115.44  E-value: 6.03e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782874   1 AVQCQNEDCATILLNFGADPDLRDIRYNTVLHYAVCGQSLSLVEKLLEYEADLEAKNKDGYTPLLVAVINNNPKMVKFLL 80
Cdd:COG0666  94 AARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLL 173

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 34782874  81 EKGADVNASDNYQRTALILAVSGEPPCLVKLLLQQG 116
Cdd:COG0666 174 EAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAG 209
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1-90 1.82e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.46  E-value: 1.82e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782874     1 AVQCQNEDCATILLNFGADPDLRDIRYNTVLHYAVCGQSLSLVEKLLEYeADLEAKNkDGYTPLLVAVINNNPKMVKFLL 80
Cdd:pfam12796   4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLL 81

                          90
                  ....*....|
gi 34782874    81 EKGADVNASD 90
Cdd:pfam12796  82 EKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 2-140 2.88e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 77.37  E-value: 2.88e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782874    2 VQCQNEDCATI---LLNFGADPDLRDIRYNTVLHYAVC-GQSLSLVEKLLEYEADLEAKNKDGYTPLLV--AVINNNPKM 75
Cdd:PHA03095  55 LHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHLYLYnATTLDVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKV 134

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 34782874   76 VKFLLEKGADVNASDNYQRTAL-ILAVS-GEPPCLVKLLLQQGVELCYegiVDsqlrnmFISMVLLH 140
Cdd:PHA03095 135 IRLLLRKGADVNALDLYGMTPLaVLLKSrNANVELLRLLIDAGADVYA---VD------DRFRSLLH 192
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 1-100 9.64e-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: 47.31  E-value: 9.64e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782874   1 AVQCQNEDCATILLNfgADPDLRDIRYN-------TVLHYAVCGQSLSLVEKLLEYEADLEA---------KNKD----- 59
Cdd:cd22192  58 AALYDNLEAAVVLME--AAPELVNEPMTsdlyqgeTALHIAVVNQNLNLVRELIARGADVVSpratgtffrPGPKnliyy 135

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 34782874  60 GYTPLLVAVINNNPKMVKFLLEKGADVNASDNYQRTAL-ILA 100
Cdd:cd22192 136 GEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLhILV 177
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 59-88 2.87e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.80  E-value: 2.87e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 34782874     59 DGYTPLLVAVINNNPKMVKFLLEKGADVNA 88
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 1-88 4.54e-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: 42.38  E-value: 4.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782874     1 AVQCQNEDCATILLNFGADPDLRDirynTVLHYAvcgqSLSLVEKLLEYEADLEAKNKDGY-----------------TP 63
Cdd:TIGR00870  60 AIENENLELTELLLNLSCRGAVGD----TLLHAI----SLEYVDAVEAILLHLLAAFRKSGplelandqytseftpgiTA 131

                          90       100
                  ....*....|....*....|....*
gi 34782874    64 LLVAVINNNPKMVKFLLEKGADVNA 88
Cdd:TIGR00870 132 LHLAAHRQNYEIVKLLLERGASVPA 156
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-116 6.03e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 115.44  E-value: 6.03e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782874   1 AVQCQNEDCATILLNFGADPDLRDIRYNTVLHYAVCGQSLSLVEKLLEYEADLEAKNKDGYTPLLVAVINNNPKMVKFLL 80
Cdd:COG0666  94 AARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLL 173

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 34782874  81 EKGADVNASDNYQRTALILAVSGEPPCLVKLLLQQG 116
Cdd:COG0666 174 EAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAG 209
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-116 3.68e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 110.43  E-value: 3.68e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782874   1 AVQCQNEDCATILLNFGADPDLRDIRYNTVLHYAVCGQSLSLVEKLLEYEADLEAKNKDGYTPLLVAVINNNPKMVKFLL 80
Cdd:COG0666 127 AAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLL 206

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 34782874  81 EKGADVNASDNYQRTALILAVSGEPPCLVKLLLQQG 116
Cdd:COG0666 207 EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
6-119 5.70e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 99.64  E-value: 5.70e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782874   6 NEDCATILLNFGADPDLRDIRYNTVLHYAVCGQSLSLVEKLLEYEADLEAKNKDGYTPLLVAVINNNPKMVKFLLEKGAD 85
Cdd:COG0666  66 DLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGAD 145

                        90       100       110
                ....*....|....*....|....*....|....
gi 34782874  86 VNASDNYQRTALILAVSGEPPCLVKLLLQQGVEL 119
Cdd:COG0666 146 VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADV 179
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-116 2.63e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 87.32  E-value: 2.63e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782874   1 AVQCQNEDCATILLNFGADPDLRDIRYNTVLHYAVCGQSLSLVEKLLEYEADLEAKNKDGYTPLLVAVINNNPKMVKFLL 80
Cdd:COG0666 160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 34782874  81 EKGADVNASDNYQRTALILAVSGEPPCLVKLLLQQG 116
Cdd:COG0666 240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLAL 275
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1-90 1.82e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.46  E-value: 1.82e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782874     1 AVQCQNEDCATILLNFGADPDLRDIRYNTVLHYAVCGQSLSLVEKLLEYeADLEAKNkDGYTPLLVAVINNNPKMVKFLL 80
Cdd:pfam12796   4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLL 81

                          90
                  ....*....|
gi 34782874    81 EKGADVNASD 90
Cdd:pfam12796  82 EKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
10-119 2.83e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 76.53  E-value: 2.83e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782874  10 ATILLNFGADPDLRDIRYNTVLHYAVCGQSLSLVEKLLEYEADLEAKNKDGYTPLLVAVINNNPKMVKFLLEKGADVNAS 89
Cdd:COG0666  37 LLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNAR 116

                        90       100       110
                ....*....|....*....|....*....|
gi 34782874  90 DNYQRTALILAVSGEPPCLVKLLLQQGVEL 119
Cdd:COG0666 117 DKDGETPLHLAAYNGNLEIVKLLLEAGADV 146
PHA03095 PHA03095
ankyrin-like protein; Provisional
 2-140 2.88e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 77.37  E-value: 2.88e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782874    2 VQCQNEDCATI---LLNFGADPDLRDIRYNTVLHYAVC-GQSLSLVEKLLEYEADLEAKNKDGYTPLLV--AVINNNPKM 75
Cdd:PHA03095  55 LHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHLYLYnATTLDVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKV 134

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 34782874   76 VKFLLEKGADVNASDNYQRTAL-ILAVS-GEPPCLVKLLLQQGVELCYegiVDsqlrnmFISMVLLH 140
Cdd:PHA03095 135 IRLLLRKGADVNALDLYGMTPLaVLLKSrNANVELLRLLIDAGADVYA---VD------DRFRSLLH 192
Ank_2 pfam12796
Ankyrin repeats (3 copies);
31-119 3.80e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 71.69  E-value: 3.80e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782874    31 LHYAVCGQSLSLVEKLLEYEADLEAKNKDGYTPLLVAVINNNPKMVKFLLEKgADVNaSDNYQRTALILAVSGEPPCLVK 110
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVN-LKDNGRTALHYAARSGHLEIVK 78


                  ....*....
gi 34782874   111 LLLQQGVEL 119
Cdd:pfam12796  79 LLLEKGADI 87
PHA03095 PHA03095
ankyrin-like protein; Provisional
 13-120 8.49e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 73.14  E-value: 8.49e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782874   13 LLNFGADPDLRDIRYNTVLHYAV---CGQSLSLVEKLLEYEADLEAKNKDGYTPLLVAVINNN-PKMVKFLLEKGADVNA 88
Cdd:PHA03095  33 LLAAGADVNFRGEYGKTPLHLYLhysSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGADVNA 112

                         90       100       110
                 ....*....|....*....|....*....|....
gi 34782874   89 SDNYQRTALILAVSGE--PPCLVKLLLQQGVELC 120
Cdd:PHA03095 113 KDKVGRTPLHVYLSGFniNPKVIRLLLRKGADVN 146
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 13-116 3.87e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 71.23  E-value: 3.87e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782874   13 LLNFGADPDLRDIRYNTVLHYAV--CGQSLSLVEKLLEYEADLEAKN--------------KD--GYTPLLVAVINNNPK 74
Cdd:PHA03100 127 LLDNGANVNIKNSDGENLLHLYLesNKIDLKILKLLIDKGVDINAKNrvnyllsygvpiniKDvyGFTPLHYAVYNNNPE 206

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 34782874   75 MVKFLLEKGADVNASDNYQRTALILAVSGEPPCLVKLLLQQG 116
Cdd:PHA03100 207 FVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNG 248
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 2-116 7.47e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 70.38  E-value: 7.47e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782874    2 VQCQNEDCATILLNFGADPDLRDIRYNTVLHYAVCGQSLSLVEKLLEYEADLEAKNKDGYTPLLVAVINNNPKMVKFLLE 81
Cdd:PHA02874  99 IPCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLE 178

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 34782874   82 KGADVNASDNYQRTALILAVS-GEPPClVKLLLQQG 116
Cdd:PHA02874 179 KGAYANVKDNNGESPLHNAAEyGDYAC-IKLLIDHG 213
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 1-118 1.63e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 69.63  E-value: 1.63e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782874    1 AVQCQNEDCATILLNFGADPDLRDIRYNTVLHYAVCGQSLSLVEKLLEYEADLEAKNKDGYTPLLVAVINNNPKMVKFLL 80
Cdd:PHA02875 109 ATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLL 188

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 34782874   81 EKGADVN-ASDNYQRTALILAVSGEPPCLVKLLLQQGVE 118
Cdd:PHA02875 189 DSGANIDyFGKNGCVAALCYAIENNKIDIVRLFIKRGAD 227
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 12-92 8.72e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 67.38  E-value: 8.72e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782874   12 ILLNFGADPDLRDIRYNTVLHYAVCGQSLSLVEKLLEYEADLEAKNKDGYTPLLVAVINNNPKMVKFLLEKGADVNASDN 91
Cdd:PHA03100 177 YLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256


                 .
gi 34782874   92 Y 92
Cdd:PHA03100 257 T 257
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 12-117 1.68e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 66.61  E-value: 1.68e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782874   12 ILLNFGADPDLRDIRYNTVLHYAVCGQS-----LSLVEKLLEYEADLEAKNKDGYTPLLVAVIN--NNPKMVKFLLEKGA 84
Cdd:PHA03100  53 ILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGA 132

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 34782874   85 DVNASDNYQRTALILAVSGEPPCL--VKLLLQQGV 117
Cdd:PHA03100 133 NVNIKNSDGENLLHLYLESNKIDLkiLKLLIDKGV 167
PHA03095 PHA03095
ankyrin-like protein; Provisional
 6-113 1.74e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 66.59  E-value: 1.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782874    6 NEDCATILLNFGADPDLRDIRYNTVLHYAVCGQSL--SLVEKLLEYEADLEAKNKDGYTPLLVAVINNNPKMVKFLLEKG 83
Cdd:PHA03095 201 RARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCkrSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALG 280

                         90       100       110
                 ....*....|....*....|....*....|
gi 34782874   84 ADVNASDNYQRTALILAVSGEPPCLVKLLL 113
Cdd:PHA03095 281 ADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 13-149 3.63e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 65.86  E-value: 3.63e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782874   13 LLNFGADPDLRDIRYNTVLHYAVCGQS-LSLVEKLLEYEADLEAKNKDGYTPLLVAVINN-NPKMVKFLLEKGADVNASD 90
Cdd:PHA02876 394 LLDYGADIEALSQKIGTALHFALCGTNpYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAIN 473

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 34782874   91 NYQRTALILAVsgEPPCLVKLLLQQGVELCYEGIVDSQLR-NMF-ISMVLLHRYPQFTASH 149
Cdd:PHA02876 474 IQNQYPLLIAL--EYHGIVNILLHYGAELRDSRVLHKSLNdNMFsFRYIIAHICIQDFIRH 532
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 5-119 2.39e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 63.54  E-value: 2.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782874    5 QNEDCATILLNFGADPDLRDIRYNTVLHYAVCGQSLSLVEKLLEYEADLEAKNKDGYTPLLVAVINNNPKM-VKFLLEKG 83
Cdd:PHA02876 353 RNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRG 432

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 34782874   84 ADVNASDNYQRTALILAVSGE-PPCLVKLLLQQGVEL 119
Cdd:PHA02876 433 ANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADV 469
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 5-142 2.04e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 60.66  E-value: 2.04e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782874    5 QNEDCATILLNFGADPDLRDIRYNTVLHYAVCGQSLSLVEKLLEYEADLEAKNKDGYTPLLVAVIN-NNPKMVKFLLEKG 83
Cdd:PHA02878 179 KDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHG 258

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 34782874   84 ADVNASdNYQRTALILAVSGEPPCLVKLLLQQGVELcyeGIVDSQlRNMFISMVLLHRY 142
Cdd:PHA02878 259 VDVNAK-SYILGLTALHSSIKSERKLKLLLEYGADI---NSLNSY-KLTPLSSAVKQYL 312
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 28-123 4.65e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 59.62  E-value: 4.65e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782874   28 NTVLHYAVCGQSLSLVEKLLEYEADLEAKNKDGYTPLLVAVINNNPKMVKFLLEKGADVNASDNYQRTALILAVSGEPPC 107
Cdd:PHA02875 103 MTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIA 182

                         90
                 ....*....|....*.
gi 34782874  108 LVKLLLQQGVELCYEG 123
Cdd:PHA02875 183 ICKMLLDSGANIDYFG 198
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 1-101 5.77e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 59.51  E-value: 5.77e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782874    1 AVQCQNEDCATILLNFGADPDLRDIRYNTVLHYAVCG-QSLSLVEKLLEYEADLEAKNK-DGYTPLLVAVinNNPKMVKF 78
Cdd:PHA02878 208 AVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYiLGLTALHSSI--KSERKLKL 285

                         90       100
                 ....*....|....*....|...
gi 34782874   79 LLEKGADVNASDNYQRTALILAV 101
Cdd:PHA02878 286 LLEYGADINSLNSYKLTPLSSAV 308
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 5-97 1.05e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 58.54  E-value: 1.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782874    5 QNEDCATILLNFGADPDLR--DIRYNTVLHYAVCGQSLS-LVEKLLEYEADLEAKNKDGYTPLLVAVINN-NPKMVKFLL 80
Cdd:PHA02876 249 RNEDLETSLLLYDAGFSVNsiDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLI 328

                         90
                 ....*....|....*..
gi 34782874   81 EKGADVNASDNYQRTAL 97
Cdd:PHA02876 329 MLGADVNAADRLYITPL 345
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 10-80 1.36e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 58.37  E-value: 1.36e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 34782874   10 ATILLNFGADPDLRDIRYNTVLHYAVCGQSLSLVEKLLEYEADLEAKNKDGYTPLLVAVINNNPKMVKFLL 80
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-97 1.80e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 57.66  E-value: 1.80e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782874   1 AVQCQNEDCATILLNFGADPDLRDIRYNTVLHYAVCGQSLSLVEKLLEYEADLEAKNKDGYTPLLVAVINNNPKMVKFLL 80
Cdd:COG0666 193 AAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLL 272

                        90
                ....*....|....*..
gi 34782874  81 EKGADVNASDNYQRTAL 97
Cdd:COG0666 273 LALLLLAAALLDLLTLL 289
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 13-116 1.13e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 55.44  E-value: 1.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782874   13 LLNFGADPDLRDIRYNTVLHYAVCGQSLSLVEKLLEYEADLEAKNKDGYTPL-----LVAVINNNPKMVKFLLEKGADVN 87
Cdd:PHA03100  21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLhylsnIKYNLTDVKEIVKLLLEYGANVN 100

                         90       100       110
                 ....*....|....*....|....*....|.
gi 34782874   88 ASDNYQRTALILAVSG--EPPCLVKLLLQQG 116
Cdd:PHA03100 101 APDNNGITPLLYAISKksNSYSIVEYLLDNG 131
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 12-117 2.65e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 54.50  E-value: 2.65e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782874   12 ILLNFGADPDLRDIRY-NTVLHYAVCGQSLSLVEKLLEYEADLEAKNKDGYTPLLVAVINNNPKMVKFLLEKGADVNASD 90
Cdd:PHA02878 152 LLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARD 231

                         90       100       110
                 ....*....|....*....|....*....|.
gi 34782874   91 NYQRTALILAVSGeppCL----VKLLLQQGV 117
Cdd:PHA02878 232 KCGNTPLHISVGY---CKdydiLKLLLEHGV 259
Ank_4 pfam13637
Ankyrin repeats (many copies);
60-113 3.05e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.97  E-value: 3.05e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 34782874    60 GYTPLLVAVINNNPKMVKFLLEKGADVNASDNYQRTALILAVSGEPPCLVKLLL 113
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
27-80 5.40e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.58  E-value: 5.40e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 34782874    27 YNTVLHYAVCGQSLSLVEKLLEYEADLEAKNKDGYTPLLVAVINNNPKMVKFLL 80
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 1-121 5.38e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 50.76  E-value: 5.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782874    1 AVQCQNEDCATILLNFGADPDLRDIRYNTVLHYAVCGQSLSLVEKLLE---YEADLEAKnkDGYTPLLVAVINNNPKMVK 77
Cdd:PHA02875  42 AMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDlgkFADDVFYK--DGMTPLHLATILKKLDIMK 119

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 34782874   78 FLLEKGADVNASDNYQRTALILAVSGEPPCLVKLLLQQ----GVELCY 121
Cdd:PHA02875 120 LLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHkaclDIEDCC 167
Ank_5 pfam13857
Ankyrin repeats (many copies);
46-100 6.31e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.57  E-value: 6.31e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 34782874    46 LLEYE-ADLEAKNKDGYTPLLVAVINNNPKMVKFLLEKGADVNASDNYQRTALILA 100
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03095 PHA03095
ankyrin-like protein; Provisional
 12-116 1.66e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 49.25  E-value: 1.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782874   12 ILLNFGADPDLRDIRYNTVLHY--AVCGQSLSLVEKLLEYEADLEAKNKDGYTPLLVAVINNNPK--MVKFLLEKGADVN 87
Cdd:PHA03095 172 LLIDAGADVYAVDDRFRSLLHHhlQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISIN 251

                         90       100
                 ....*....|....*....|....*....
gi 34782874   88 ASDNYQRTALILAVSGEPPCLVKLLLQQG 116
Cdd:PHA03095 252 ARNRYGQTPLHYAAVFNNPRACRRLIALG 280
PHA02798 PHA02798
ankyrin-like protein; Provisional
 8-119 1.70e-07

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 49.45  E-value: 1.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782874    8 DCATILLNFGADPDLRDIRYNTVL-----HYAVCGQSLSLVEKLLEYEADLEAKNKDGYTPLLVAVIN---NNPKMVKFL 79
Cdd:PHA02798  52 DIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNgyiNNLEILLFM 131

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 34782874   80 LEKGADVNASDNYQRTALILAVSGEPPC---LVKLLLQQGVEL 119
Cdd:PHA02798 132 IENGADTTLLDKDGFTMLQVYLQSNHHIdieIIKLLLEKGVDI 174
Ank_5 pfam13857
Ankyrin repeats (many copies);
12-67 4.19e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.64  E-value: 4.19e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 34782874    12 ILLNFGADPDLRDIRYNTVLHYAVCGQSLSLVEKLLEYEADLEAKNKDGYTPLLVA 67
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 59-88 4.76e-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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 43.79  E-value: 4.76e-07
                          10        20        30
                  ....*....|....*....|....*....|
gi 34782874    59 DGYTPLLVAVINNNPKMVKFLLEKGADVNA 88
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 59-91 8.97e-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: 43.05  E-value: 8.97e-07
                          10        20        30
                  ....*....|....*....|....*....|....
gi 34782874    59 DGYTPLLVAVI-NNNPKMVKFLLEKGADVNASDN 91
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 1-100 9.64e-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: 47.31  E-value: 9.64e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782874   1 AVQCQNEDCATILLNfgADPDLRDIRYN-------TVLHYAVCGQSLSLVEKLLEYEADLEA---------KNKD----- 59
Cdd:cd22192  58 AALYDNLEAAVVLME--AAPELVNEPMTsdlyqgeTALHIAVVNQNLNLVRELIARGADVVSpratgtffrPGPKnliyy 135

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 34782874  60 GYTPLLVAVINNNPKMVKFLLEKGADVNASDNYQRTAL-ILA 100
Cdd:cd22192 136 GEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLhILV 177
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
12-119 1.75e-06

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 46.10  E-value: 1.75e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782874  12 ILLNFGADPDLRDIRYNTVLHYAVCGQSLSLVEKLLEYEADLEAKNKDGYTPLLVAVINNNPKMVKFLLEKGADVNASDN 91
Cdd:COG0666   6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85

                        90       100
                ....*....|....*....|....*...
gi 34782874  92 YQRTALILAVSGEPPCLVKLLLQQGVEL 119
Cdd:COG0666  86 GGNTLLHAAARNGDLEIVKLLLEAGADV 113
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 39-117 2.17e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 46.20  E-value: 2.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782874   39 SLSLVEKLLEYEADLEAKNKDGYTPLLVAVINNNPKMVKFLLEKGADVNASDNYQRTALIL-----AVSGEPPCLVKLLL 113
Cdd:PHA03100  14 KVKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYlsnikYNLTDVKEIVKLLL 93


                 ....
gi 34782874  114 QQGV 117
Cdd:PHA03100  94 EYGA 97
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 59-88 2.87e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.80  E-value: 2.87e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 34782874     59 DGYTPLLVAVINNNPKMVKFLLEKGADVNA 88
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 7-141 3.23e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 45.63  E-value: 3.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782874    7 EDCATILLNFGADPDLRDIRYNTVLHYAVCGQSLSLVEKLLEYeadleAKNKDGYTP---LLVAVINNNPKMVKFLLEKG 83
Cdd:PLN03192 571 EDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHF-----ASISDPHAAgdlLCTAAKRNDLTAMKELLKQG 645

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 34782874   84 ADVNASDNYQRTALILAVSGEPPCLVKLLLQQGVEL----CYEGIVDSQLRNMFISMVLLHR 141
Cdd:PLN03192 646 LNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVdkanTDDDFSPTELRELLQKRELGHS 707
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 10-104 5.01e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.05  E-value: 5.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782874   10 ATILLNFGADPDLRDIRYNTVLHYAVCGQSLSLVEKLLEYEADLEAKNKDGYTPLLVAVINNNPKMVKFLLEKGADVNAS 89
Cdd:PHA02876 161 AEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKN 240

                         90
                 ....*....|....*
gi 34782874   90 DnyqrTALILAVSGE 104
Cdd:PHA02876 241 D----LSLLKAIRNE 251
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 32-118 6.71e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.89  E-value: 6.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782874   32 HYAVCGQSLSlVEKLLEYEADLEAKNKDGYTPLLVAVINNNPKMVKFLLEKGADVNASDNYQRTALILAVSGEPPCLVKL 111
Cdd:PTZ00322  88 QLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                 ....*..
gi 34782874  112 LLQQGVE 118
Cdd:PTZ00322 167 LSRHSQC 173
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 8-86 1.05e-05

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: 44.23  E-value: 1.05e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782874   8 DCATI---LLNFGADPDLRDIRYNTVLHYAVCGQSLSLVEKLLEYEADL--EAKNKD---GYTPLLVAVINNNPKMVKFL 79
Cdd:cd22192  29 DVQAIkklLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELvnEPMTSDlyqGETALHIAVVNQNLNLVREL 108


                ....*..
gi 34782874  80 LEKGADV 86
Cdd:cd22192 109 IARGADV 115
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 4-82 2.15e-05

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: 43.08  E-value: 2.15e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782874   4 CQ-NEDCATILLNFGADPDLRDIRYNTVLHYAVCGQSLSLV----EKLLEYEADLEA------KNKDGYTPLLVAVINNN 72
Cdd:cd22192 145 CVgNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFAcqmyDLILSYDKEDDLqpldlvPNNQGLTPFKLAAKEGN 224

                        90
                ....*....|
gi 34782874  73 PKMVKFLLEK 82
Cdd:cd22192 225 IVMFQHLVQK 234
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 1-101 3.95e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 42.26  E-value: 3.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782874    1 AVQCQNEDCATILLNFGADPDLRDIRYNTVLHYAVCGQSLSLVEKLLEYEADLEAKNKDGYTPLLVAVINNNPKMVKFLL 80
Cdd:PHA02874 131 AIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLI 210

                         90       100
                 ....*....|....*....|.
gi 34782874   81 EKGADVNASDNYQRTALILAV 101
Cdd:PHA02874 211 DHGNHIMNKCKNGFTPLHNAI 231
PHA03095 PHA03095
ankyrin-like protein; Provisional
 10-91 4.37e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 42.32  E-value: 4.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782874   10 ATILLNF---GADPDLRDIRYNTVLHYAVCGQSLSLVEKLLEYEADLEAKNKDGYTPLLVAVINNNPKMVKFLLEKGADV 86
Cdd:PHA03095 237 RSLVLPLliaGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSA 316


                 ....*
gi 34782874   87 NASDN 91
Cdd:PHA03095 317 ETVAA 321
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 1-88 4.54e-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: 42.38  E-value: 4.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782874     1 AVQCQNEDCATILLNFGADPDLRDirynTVLHYAvcgqSLSLVEKLLEYEADLEAKNKDGY-----------------TP 63
Cdd:TIGR00870  60 AIENENLELTELLLNLSCRGAVGD----TLLHAI----SLEYVDAVEAILLHLLAAFRKSGplelandqytseftpgiTA 131

                          90       100
                  ....*....|....*....|....*
gi 34782874    64 LLVAVINNNPKMVKFLLEKGADVNA 88
Cdd:TIGR00870 132 LHLAAHRQNYEIVKLLLERGASVPA 156
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 28-116 9.70e-05

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 41.15  E-value: 9.70e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782874  28 NTVLHYAVCGQSLSLVEKLLEYE-ADLEAKNKDGYTPLLVAVINNNPKMVKFLLEKGAD-VN---ASDNYQ-RTALILAV 101
Cdd:cd22192  18 ESPLLLAAKENDVQAIKKLLKCPsCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNepmTSDLYQgETALHIAV 97

                        90
                ....*....|....*
gi 34782874 102 SGEPPCLVKLLLQQG 116
Cdd:cd22192  98 VNQNLNLVRELIARG 112
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 26-97 1.34e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. 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: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 40.94  E-value: 1.34e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782874  26 RYNTVLHYAVCGQSLSLVEKLLEYEADLEA----------KNKDGY----TPLLVAVINNNPKMVKFLLE---KGADVNA 88
Cdd:cd22196  93 KGQTALHIAIERRNMHLVELLVQNGADVHArasgeffkkkKGGPGFyfgeLPLSLAACTNQLDIVKFLLEnphSPADISA 172


                ....*....
gi 34782874  89 SDNYQRTAL 97
Cdd:cd22196 173 RDSMGNTVL 181
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 1-107 1.82e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 40.33  E-value: 1.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782874    1 AVQCQNEDCATILLNFGADPDLRDIRYNTVLHYAVCGQSLSLVEKLLEYEADLEAKNKDGYTPLLVAVINNnpKMVKFLL 80
Cdd:PHA02874 164 AIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHN--RSAIELL 241

                         90       100
                 ....*....|....*....|....*..
gi 34782874   81 EKGADVNASDNYQRTALILAVsgEPPC 107
Cdd:PHA02874 242 INNASINDQDIDGSTPLHHAI--NPPC 266
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 8-133 2.02e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong 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: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 40.55  E-value: 2.02e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782874   8 DCATILLNFGADPD---------LRDIRY--NTVLHYAVCGQSLSLVEKLLEYEADLEAKNKD--------------GYT 62
Cdd:cd22193  46 DTIRILLDIAEKTDnlkrfinaeYTDEYYegQTALHIAIERRQGDIVALLVENGADVHAHAKGrffqpkyqgegfyfGEL 125

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782874  63 PLLVAVINNNPKMVKFLLE---KGADVNASDNYQRTALILAV-----SGEPPCLVK----LLLQQGVELCyegiVDSQLR 130
Cdd:cd22193 126 PLSLAACTNQPDIVQYLLEnehQPADIEAQDSRGNTVLHALVtvadnTKENTKFVTrmydMILIRGAKLC----PTVELE 201


                ...
gi 34782874 131 NMF 133
Cdd:cd22193 202 EIR 204
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 8-100 2.41e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 39.97  E-value: 2.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782874    8 DCATILLNFGADPD----LRDIRYNTVLHYAVCGQSLSLVEKLLEYEADLEA-KNKDGYTPLLVAVINNNPKMVKFLLEK 82
Cdd:PHA02884  47 DIIDAILKLGADPEapfpLSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRyAEEAKITPLYISVLHGCLKCLEILLSY 126

                         90
                 ....*....|....*...
gi 34782874   83 GADVNASDNYQRTALILA 100
Cdd:PHA02884 127 GADINIQTNDMVTPIELA 144
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 23-87 6.18e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 38.89  E-value: 6.18e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 34782874   23 RDIRYNTVLHYAVCGQSLSLVEKLLEYEADLEAKNKDGYTPLLVAVINNNPKMVKFLLEKGADVN 87
Cdd:PHA02876 141 ESIEYMKLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVN 205
Ank_4 pfam13637
Ankyrin repeats (many copies);
6-47 6.63e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.10  E-value: 6.63e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 34782874     6 NEDCATILLNFGADPDLRDIRYNTVLHYAVCGQSLSLVEKLL 47
Cdd:pfam13637  13 HLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02946 PHA02946
ankyin-like protein; Provisional
 42-119 9.17e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 38.50  E-value: 9.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782874   42 LVEKLLEYEADLEAKNKDGYTPLLVAVINNNPKMVKFLLEKGADVNASDNYQRTALILAVSGEPPCL--VKLLLQQGVEL 119
Cdd:PHA02946  54 FVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIerINLLVQYGAKI 133
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 60-127 9.32e-04

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: 38.32  E-value: 9.32e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782874  60 GYTPLLVAVINNNPKMVKFLLEKGADVNASDN---YQRTALILAVSGEPP-----C-----LVKLLLQQGVELCYEGIVD 126
Cdd:cd21882  73 GQTALHIAIENRNLNLVRLLVENGADVSARATgrfFRKSPGNLFYFGELPlslaaCtnqeeIVRLLLENGAQPAALEAQD 152


                .
gi 34782874 127 S 127
Cdd:cd21882 153 S 153
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 29-120 1.16e-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: 38.32  E-value: 1.16e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782874  29 TVLHYAVCGQSLSLVEKLLEYEADLEAKNKD-------------GYTPLLVAVINNNPKMVKFLLEKGAD---VNASDNY 92
Cdd:cd21882  75 TALHIAIENRNLNLVRLLVENGADVSARATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQpaaLEAQDSL 154

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 34782874  93 QRT---ALILAVSGEPPC------LVKLLLQQGVELC 120
Cdd:cd21882 155 GNTvlhALVLQADNTPENsafvcqMYNLLLSYGAHLD 191
TRPV4 cd22195
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed ...
 22-97 1.39e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed broadly in neuronal and non-neuronal cells. It is activated by various stimuli, including hypo-osmolarity, warm temperature, and chemical ligands. TRPV4 acts in physiological functions such as osmoregulation and thermoregulation. It also has a role in mechanosensation in the vascular endothelium and urinary tract, and in cell barrier formation in vascular and epidermal tissues. Knockout mice studies suggested the functional importance of TRPV4 in the central nervous system, nociception, and bone formation. TRPV4 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: 411979 [Multi-domain]  Cd Length: 733  Bit Score: 37.91  E-value: 1.39e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782874  22 LRDIRY--NTVLHYAVCGQSLSLVEKLLEYEADLEA---------KNKDGY-----TPLLVAVINNNPKMVKFLLE---K 82
Cdd:cd22195 130 FRDVYYrgQTALHIAIERRCKHYVELLVEKGADVHAqargrffqpKDEGGYfyfgeLPLSLAACTNQPDIVHYLTEnahK 209

                        90
                ....*....|....*
gi 34782874  83 GADVNASDNYQRTAL 97
Cdd:cd22195 210 KADLRRQDSRGNTVL 224
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 40-118 1.69e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 37.64  E-value: 1.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782874   40 LSLVEKLLEYEAD-LEAKNKDGYTPLLVAVINNNPKMVKFLLEKGADVNASDNYQRTALILAVSGEPPCLVKLLLQQGVE 118
Cdd:PHA02874  14 IEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVD 93
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 7-89 1.73e-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: 37.82  E-value: 1.73e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782874   7 EDCATILLNFGADPDLRDIRYN-----------TVLHYAVCGQSLSLVEKLLEYEADLEAKNK----------DGY---- 61
Cdd:cd22194 110 KEIVRILLAFAEENGILDRFINaeyteeayegqTALNIAIERRQGDIVKLLIAKGADVNAHAKgvffnpkykhEGFyfge 189

                        90       100
                ....*....|....*....|....*...
gi 34782874  62 TPLLVAVINNNPKMVKFLLEKGADVNAS 89
Cdd:cd22194 190 TPLALAACTNQPEIVQLLMEKESTDITS 217
PHA02741 PHA02741
hypothetical protein; Provisional
 12-98 1.86e-03

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 36.94  E-value: 1.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782874   12 ILLNFGADPDLRD-IRYNTVLHYAVCGQSLSLVEKLL-EYEADLEAKNKDGYTPLLVAVINNNPKMVKFLLEKGADVNAS 89
Cdd:PHA02741  82 HLIELGADINAQEmLEGDTALHLAAHRRDHDLAEWLCcQPGIDLHFCNADNKSPFELAIDNEDVAMMQILREIVATSRGF 161


                 ....*....
gi 34782874   90 DNyQRTALI 98
Cdd:PHA02741 162 SN-ENTDIV 169
PHA02798 PHA02798
ankyrin-like protein; Provisional
 8-91 3.01e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 36.74  E-value: 3.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782874    8 DCATILLNFGADPDLRDIRYNTVLHYAVCGQSLSLVEKLL---EYEADLEAKNKDGYTPLLVAVINNNP---KMVKFLLE 81
Cdd:PHA02798  90 DIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLfmiENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLE 169

                         90
                 ....*....|
gi 34782874   82 KGADVNASDN 91
Cdd:PHA02798 170 KGVDINTHNN 179
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 42-119 3.07e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 37.03  E-value: 3.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782874   42 LVEKLLEYEADLEAKNKDGYTPLLVAVIN---NNPKMVKFLLEKGADVNASDNYqRTALILAVSGEPPC----LVKLLLQ 114
Cdd:PHA02989  90 IVKLLLKFGADINLKTFNGVSPIVCFIYNsniNNCDMLRFLLSKGINVNDVKNS-RGYNLLHMYLESFSvkkdVIKILLS 168


                 ....*
gi 34782874  115 QGVEL 119
Cdd:PHA02989 169 FGVNL 173
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 51-116 4.12e-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: 36.66  E-value: 4.12e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782874  51 ADLEAKNKDGYTPLLVAVINNNPKMVKFLLEKGADVNA---------SDNYQ-----RTALILAVSGEPPCLVKLLLQQG 116
Cdd:cd22194 132 AEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAhakgvffnpKYKHEgfyfgETPLALAACTNQPEIVQLLMEKE 211
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 12-84 4.97e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 35.62  E-value: 4.97e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 34782874   12 ILLNFGADPDLRD-IRYNTVLHYAVCGQSLSLVEKLLEY-EADLEAKNKDGYTPLLVAVINNNPKMVKFLLEKGA 84
Cdd:PHA02736  76 LLMEWGADINGKErVFGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGA 150
 
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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