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Conserved domains on  [gi|1280409835|ref|NP_001345345|]
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putative ankyrin repeat domain-containing protein 30B-like [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];
35-202 7.08e-34

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 123.91  E-value: 7.08e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835  35 HHGDLRKIHKAASRGQAWKLERMMKKTTMDLNIRDAKKRTALYWACANGHAEVVTLLVDRKCQLDVLDGENRTILMKALQ 114
Cdd:COG0666    50 ADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAY 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835 115 CQREACANILIDSGADPNIVDVYGNTAVHYAVNSENLSVVAKLLSCGADIEVKNKAGHTPLLLAIRKRSEEIVEFLLTKN 194
Cdd:COG0666   130 NGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAG 209


                  ....*...
gi 1280409835 195 ANANAVDK 202
Cdd:COG0666   210 ADVNAKDN 217
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
35-202 7.08e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 123.91  E-value: 7.08e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835  35 HHGDLRKIHKAASRGQAWKLERMMKKTTMDLNIRDAKKRTALYWACANGHAEVVTLLVDRKCQLDVLDGENRTILMKALQ 114
Cdd:COG0666    50 ADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAY 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835 115 CQREACANILIDSGADPNIVDVYGNTAVHYAVNSENLSVVAKLLSCGADIEVKNKAGHTPLLLAIRKRSEEIVEFLLTKN 194
Cdd:COG0666   130 NGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAG 209


                  ....*...
gi 1280409835 195 ANANAVDK 202
Cdd:COG0666   210 ADVNAKDN 217
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 64-203 2.09e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 83.56  E-value: 2.09e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835  64 DLNIRDAKKRTALYWACAN--GHAEVVTLLVDRKCQLDVLDGENRTILMKALQCQRE----------------ACANI-- 123
Cdd:PHA03100   98 NVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlkilkllidkgvdinAKNRVny 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835 124 LIDSGADPNIVDVYGNTAVHYAVNSENLSVVAKLLSCGADIEVKNKAGHTPLLLAIRKRSEEIVEFLLTKNANANAVDKF 203
Cdd:PHA03100  178 LLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
Ank_2 pfam12796
Ankyrin repeats (3 copies);
76-168 3.45e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.38  E-value: 3.45e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835  76 LYWACANGHAEVVTLLVDRKCQLDVLDGENRTILMKALQCQREACANILIDSgADPNIVDvYGNTAVHYAVNSENLSVVA 155
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1280409835 156 KLLSCGADIEVKN 168
Cdd:pfam12796  79 LLLEKGADINVKD 91
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 45-203 1.15e-06

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: 49.24  E-value: 1.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835  45 AASRGQAWKLERMMKKTTMDLNIRDAKKRTALYWACANGHAEVVTLLVDrkcqldvldgenrtilmkalqcqreaCANIL 124
Cdd:cd22192    24 AAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--------------------------AAPEL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835 125 IDsgaDPNIVDVY-GNTAVHYAVNSENLSVVAKLLSCGADIeVKNKA---------------GHTPLLLAIRKRSEEIVE 188
Cdd:cd22192    78 VN---EPMTSDLYqGETALHIAVVNQNLNLVRELIARGADV-VSPRAtgtffrpgpknliyyGEHPLSFAACVGNEEIVR 153

                         170
                  ....*....|....*
gi 1280409835 189 FLLTKNANANAVDKF 203
Cdd:cd22192   154 LLIEHGADIRAQDSL 168
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 40-203 5.73e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 40.83  E-value: 5.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835  40 RKIHKAASRGQAWKLERMMKKTTMD-LNIRDAKKRTALYWACA-NGHAEVVTLLVDRKCQLDVLDgenrTILMKA-LQCQ 116
Cdd:TIGR00870  19 KAFLPAAERGDLASVYRDLEEPKKLnINCPDRLGRSALFVAAIeNENLELTELLLNLSCRGAVGD----TLLHAIsLEYV 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835 117 R--EACANILI----DSGADPNIVDVYGN------TAVHYAVNSENLSVVAKLLSCGADIEVKNKA-------------- 170
Cdd:TIGR00870  95 DavEAILLHLLaafrKSGPLELANDQYTSeftpgiTALHLAAHRQNYEIVKLLLERGASVPARACGdffvksqgvdsfyh 174

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1280409835 171 GHTPLLLAIRKRSEEIVEFLLTKNANANAVDKF 203
Cdd:TIGR00870 175 GESPLNAAACLGSPSIVALLSEDPADILTADSL 207
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 137-166 1.40e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.26  E-value: 1.40e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1280409835  137 YGNTAVHYAVNSENLSVVAKLLSCGADIEV 166
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
35-202 7.08e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 123.91  E-value: 7.08e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835  35 HHGDLRKIHKAASRGQAWKLERMMKKTTMDLNIRDAKKRTALYWACANGHAEVVTLLVDRKCQLDVLDGENRTILMKALQ 114
Cdd:COG0666    50 ADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAY 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835 115 CQREACANILIDSGADPNIVDVYGNTAVHYAVNSENLSVVAKLLSCGADIEVKNKAGHTPLLLAIRKRSEEIVEFLLTKN 194
Cdd:COG0666   130 NGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAG 209


                  ....*...
gi 1280409835 195 ANANAVDK 202
Cdd:COG0666   210 ADVNAKDN 217
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
42-202 1.31e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 123.14  E-value: 1.31e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835  42 IHKAASRGQAwKLERMMKKTTMDLNIRDAKKRTALYWACANGHAEVVTLLVDRKCQLDVLDGENRTILMKALQCQREACA 121
Cdd:COG0666    91 LHAAARNGDL-EIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835 122 NILIDSGADPNIVDVYGNTAVHYAVNSENLSVVAKLLSCGADIEVKNKAGHTPLLLAIRKRSEEIVEFLLTKNANANAVD 201
Cdd:COG0666   170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKD 249


                  .
gi 1280409835 202 K 202
Cdd:COG0666   250 K 250
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
24-202 3.41e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 108.89  E-value: 3.41e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835  24 LVYTNNDSYVIHHGDLRKIHKAASRGQAWKLERMMKKTTMDLNIRDAKKRTALYWACANGHAEVVTLLVDRKCQLDVLDG 103
Cdd:COG0666     6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835 104 ENRTILMKALQCQREACANILIDSGADPNIVDVYGNTAVHYAVNSENLSVVAKLLSCGADIEVKNKAGHTPLLLAIRKRS 183
Cdd:COG0666    86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165

                         170
                  ....*....|....*....
gi 1280409835 184 EEIVEFLLTKNANANAVDK 202
Cdd:COG0666   166 LEIVKLLLEAGADVNARDN 184
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
64-204 1.74e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 104.27  E-value: 1.74e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835  64 DLNIRDAKKRTALYWACANGHAEVVTLLVDRKCQLDVLDGENRTILMKALQCQREACANILIDSGADPNIVDVYGNTAVH 143
Cdd:COG0666   145 DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALD 224

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1280409835 144 YAVNSENLSVVAKLLSCGADIEVKNKAGHTPLLLAIRKRSEEIVEFLLTKNANANAVDKFK 204
Cdd:COG0666   225 LAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 64-203 2.09e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 83.56  E-value: 2.09e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835  64 DLNIRDAKKRTALYWACAN--GHAEVVTLLVDRKCQLDVLDGENRTILMKALQCQRE----------------ACANI-- 123
Cdd:PHA03100   98 NVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlkilkllidkgvdinAKNRVny 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835 124 LIDSGADPNIVDVYGNTAVHYAVNSENLSVVAKLLSCGADIEVKNKAGHTPLLLAIRKRSEEIVEFLLTKNANANAVDKF 203
Cdd:PHA03100  178 LLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
Ank_2 pfam12796
Ankyrin repeats (3 copies);
76-168 3.45e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.38  E-value: 3.45e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835  76 LYWACANGHAEVVTLLVDRKCQLDVLDGENRTILMKALQCQREACANILIDSgADPNIVDvYGNTAVHYAVNSENLSVVA 155
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1280409835 156 KLLSCGADIEVKN 168
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
42-135 2.92e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 71.69  E-value: 2.92e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835  42 IHKAASRGQAWKLERMMKKTTmDLNIRDAKKRTALYWACANGHAEVVTLLVDRKCQLDVLDGenRTILMKALQCQREACA 121
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGA-DANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNG--RTALHYAARSGHLEIV 77

                          90
                  ....*....|....
gi 1280409835 122 NILIDSGADPNIVD 135
Cdd:pfam12796  78 KLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
109-201 3.04e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 71.69  E-value: 3.04e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835 109 LMKALQCQREACANILIDSGADPNIVDVYGNTAVHYAVNSENLSVVAKLLSCgADIEVKNKaGHTPLLLAIRKRSEEIVE 188
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1280409835 189 FLLTKNANANAVD 201
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 42-203 4.34e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 74.33  E-value: 4.34e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835  42 IHKAASRGQAwKLERMMKKTTMDLNIRDAKKRTALYWACANGHAEVVTLLVDRKCQLDvldgENRTILMKALQCQREACA 121
Cdd:PHA02876  182 IHYAAERGNA-KMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNIN----KNDLSLLKAIRNEDLETS 256

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835 122 NILIDSGADPNIVDVYGNTAVHYAVNSENLS-VVAKLLSCGADIEVKNKAGHTPL-LLAIRKRSEEIVEFLLTKNANANA 199
Cdd:PHA02876  257 LLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLyLMAKNGYDTENIRTLIMLGADVNA 336


                  ....
gi 1280409835 200 VDKF 203
Cdd:PHA02876  337 ADRL 340
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 64-204 3.85e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 71.45  E-value: 3.85e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835  64 DLNIRDAKK-RTALYWACANGHAEVVTLLVDRKCQLDVLDGENRTILMKALQCQREACANILIDSGADPNIVDVYGNTAV 142
Cdd:PHA02878  159 DINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPL 238

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1280409835 143 HYAVNS-ENLSVVAKLLSCGADIEVKNKA-GHTPLLLAIrkRSEEIVEFLLTKNANANAVDKFK 204
Cdd:PHA02878  239 HISVGYcKDYDILKLLLEHGVDVNAKSYIlGLTALHSSI--KSERKLKLLLEYGADINSLNSYK 300
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 54-201 4.86e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 68.07  E-value: 4.86e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835  54 LERMMKKTTMD----LNIRDAKKRTALYWACANGHAEVVTLLVDRKCQLDVLDGENRTILMKALQCQREACANILIDSGA 129
Cdd:PHA02874  102 IEKDMIKTILDcgidVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGA 181

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1280409835 130 DPNIVDVYGNTAVHYAVNSENLSVVAKLLSCGADIEVKNKAGHTPLLLAI-RKRSeeIVEfLLTKNANANAVD 201
Cdd:PHA02874  182 YANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIiHNRS--AIE-LLINNASINDQD 251
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 45-216 2.59e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 66.43  E-value: 2.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835  45 AASRGQAWKLERMMKkTTMDLNIRDAKKRTALYWACANGHAEVVTLLVDRKCQLDVLDGENRTILMKALQCQREACANIL 124
Cdd:PLN03192  532 VASTGNAALLEELLK-AKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835 125 --IDSGADPNIvdvyGNTAVHYAVNSENLSVVAKLLSCGADIEVKNKAGHTPLLLAIRKRSEEIVEFLLTKNAN---ANA 199
Cdd:PLN03192  611 yhFASISDPHA----AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADvdkANT 686

                         170
                  ....*....|....*..
gi 1280409835 200 VDKFKcvHQQLLEYKQK 216
Cdd:PLN03192  687 DDDFS--PTELRELLQK 701
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 86-226 3.63e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 65.46  E-value: 3.63e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835  86 EVVTLLVDRKCQLDVLDGENRTILMKALQCQREACANI--LIDSGADPNIVDVYGNTAVHYAV--NSENLSVVAKLLSCG 161
Cdd:PHA03100   87 EIVKLLLEYGANVNAPDNNGITPLLYAISKKSNSYSIVeyLLDNGANVNIKNSDGENLLHLYLesNKIDLKILKLLIDKG 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835 162 ADIEVKNKA----------------GHTPLLLAIRKRSEEIVEFLLTKNANANAVDKF--KCVHQQLLEYKQKISKNSQN 223
Cdd:PHA03100  167 VDINAKNRVnyllsygvpinikdvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYgdTPLHIAILNNNKEIFKLLLN 246


                  ...
gi 1280409835 224 SNP 226
Cdd:PHA03100  247 NGP 249
PHA03095 PHA03095
ankyrin-like protein; Provisional
 105-205 4.24e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 65.43  E-value: 4.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835 105 NRTILMKALQCQREACANI---LIDSGADPNIVDVYGNTAVH-YAVNSENLSVVAKLLSCGADIEVKNKAGHTPLLLAIR 180
Cdd:PHA03095   47 GKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVYLS 126

                          90       100
                  ....*....|....*....|....*..
gi 1280409835 181 KRS--EEIVEFLLTKNANANAVDKFKC 205
Cdd:PHA03095  127 GFNinPKVIRLLLRKGADVNALDLYGM 153
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 64-226 1.11e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 63.92  E-value: 1.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835  64 DLNIRDAKKRTALYWACANGHAEVVTLLVDRKCQLDVLDGENRTILMKALQCQREACAN-----ILIDSGADPNIVDVYG 138
Cdd:PHA03100   27 LNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLTDVkeivkLLLEYGANVNAPDNNG 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835 139 NTAVHYAVN--SENLSVVAKLLSCGADIEVKNKAGHTPLLLAIR--KRSEEIVEFLLTKNANANAVDKFKCvhqqLLEYK 214
Cdd:PHA03100  107 ITPLLYAISkkSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLEsnKIDLKILKLLIDKGVDINAKNRVNY----LLSYG 182

                         170
                  ....*....|...
gi 1280409835 215 QKI-SKNSQNSNP 226
Cdd:PHA03100  183 VPInIKDVYGFTP 195
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 54-201 1.69e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 63.44  E-value: 1.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835  54 LERMMKKTTMDLNIRDAKKRTALYWACANGHAEVVTLLVDRKCQLDVLDGENRTILMKALQ------------------- 114
Cdd:PHA02874   17 IEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKigahdiikllidngvdtsi 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835 115 ----CQREACANILIDSGADPNIVDVYGNTAVHYAVNSENLSVVAKLLSCGADIEVKNKAGHTPLLLAIRKRSEEIVEFL 190
Cdd:PHA02874   97 lpipCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLL 176

                         170
                  ....*....|.
gi 1280409835 191 LTKNANANAVD 201
Cdd:PHA02874  177 LEKGAYANVKD 187
PHA03095 PHA03095
ankyrin-like protein; Provisional
 68-202 8.00e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 61.58  E-value: 8.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835  68 RDAKKRTALYWACANGH--AEVVTLLVDRKCQLDVLDGENRTIL-MKALQCqreACANI----LIDSGADPNIVDVYGNT 140
Cdd:PHA03095  183 VDDRFRSLLHHHLQSFKprARIVRELIRAGCDPAATDMLGNTPLhSMATGS---SCKRSlvlpLLIAGISINARNRYGQT 259

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1280409835 141 AVHYAVNSENLSVVAKLLSCGADIEVKNKAGHTPLLLAIRKRSEEIVEFLLTKNANANAVDK 202
Cdd:PHA03095  260 PLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAA 321
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 121-212 1.50e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 61.07  E-value: 1.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835 121 ANILIDSGADPNIVDVYGNTAVHYAVNSENLSVVAKLLSCGADIEVKNKAGHTPLLLAIRKRSEEIVEFLLT-----KNA 195
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRhsqchFEL 177

                          90
                  ....*....|....*...
gi 1280409835 196 NANAV-DKFKCVHQQLLE 212
Cdd:PTZ00322  178 GANAKpDSFTGKPPSLED 195
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 42-200 2.06e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 60.39  E-value: 2.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835  42 IHKAASRGQAWKLERMMKKTTMDLNIRDAKKRTALYWACANGHAEVVTLLVDRKCQLDVLDGENRTILMKALQCQREACA 121
Cdd:PHA02875   72 LHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGI 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835 122 NILIDSGADPNIVDVYGNTAVHYAVNSENLSVVAKLLSCGADIEVKNKAGHTPLL-LAIRKRSEEIVEFLLTKNANANAV 200
Cdd:PHA02875  152 ELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALcYAIENNKIDIVRLFIKRGADCNIM 231
Ank_2 pfam12796
Ankyrin repeats (3 copies);
143-202 7.43e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 54.35  E-value: 7.43e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835 143 HYAVNSENLSVVAKLLSCGADIEVKNKAGHTPLLLAIRKRSEEIVEFLLtKNANANAVDK 202
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDN 60
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 123-203 1.16e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 57.97  E-value: 1.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835 123 ILIDSGADPNIVDVY-GNTAVHYAVNSENLSVVAKLLSCGADIEVKNKAGHTPLLLAIRKRSEEIVEFLLTKNANANAVD 201
Cdd:PHA02878  152 LLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARD 231


                  ..
gi 1280409835 202 KF 203
Cdd:PHA02878  232 KC 233
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 66-206 1.04e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 55.00  E-value: 1.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835  66 NIRDAKKRTALYWACANGHAEVVTLLVD-RKCQLDVLDGENRTILMKALQCQREACANILIDSGADPNIVDVYGNTAVHY 144
Cdd:PHA02875   62 DVKYPDIESELHDAVEEGDVKAVEELLDlGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHL 141

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1280409835 145 AVNSENLSVVAKLLSCGADIEVKNKAGHTPLLLAIRKRSEEIVEFLLTKNANANAVDKFKCV 206
Cdd:PHA02875  142 AVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCV 203
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 50-203 1.89e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 54.68  E-value: 1.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835  50 QAWKLERMMKKTT---MDLNIRDAKKRTALYWACANGH-AEVVTLLVDRKCQLDVLDGENRTILMKALQCQREACANI-L 124
Cdd:PHA02876  282 QAPSLSRLVPKLLergADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIVItL 361

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835 125 IDSGADPNIVDVYGNTAVHYAVNSENLSVVAKLLSCGADIEVKNKAGHTPLLLAIRKRSEEI-VEFLLTKNANANAVDKF 203
Cdd:PHA02876  362 LELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVNSKNKD 441
Ank_4 pfam13637
Ankyrin repeats (many copies);
138-191 8.23e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.65  E-value: 8.23e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1280409835 138 GNTAVHYAVNSENLSVVAKLLSCGADIEVKNKAGHTPLLLAIRKRSEEIVEFLL 191
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 64-203 8.27e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 52.33  E-value: 8.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835  64 DLNIRDAKKRTAL-YWACANGHAEVVTLLVDRKCQLDVLDGENRTILMKAL--QCQREACANILIDSGADPNIVDVYGNT 140
Cdd:PHA03095   75 DVNAPERCGFTPLhLYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVYLsgFNINPKVIRLLLRKGADVNALDLYGMT 154

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1280409835 141 AVHYAVNSENLSV--VAKLLSCGADIEVKNKAGHTPL---LLAIRKRsEEIVEFLLTKNANANAVDKF 203
Cdd:PHA03095  155 PLAVLLKSRNANVelLRLLIDAGADVYAVDDRFRSLLhhhLQSFKPR-ARIVRELIRAGCDPAATDML 221
PHA03095 PHA03095
ankyrin-like protein; Provisional
 124-203 2.05e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 51.18  E-value: 2.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835 124 LIDSGADPNIVDVYGNTAVHYAVNSEN---LSVVAKLLSCGADIEVKNKAGHTPLLLAIR-KRSEEIVEFLLTKNANANA 199
Cdd:PHA03095   33 LLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYnATTLDVIKLLIKAGADVNA 112


                  ....
gi 1280409835 200 VDKF 203
Cdd:PHA03095  113 KDKV 116
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 64-191 4.26e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 50.45  E-value: 4.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835  64 DLNIRDAKKRTALYWACANGHAEVVTLLVDRKCQLDVLDGENRTILMKALqCQREACANI--LIDSGADPNIVDVYGNTA 141
Cdd:PHA02876  367 NVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAL-CGTNPYMSVktLIDRGANVNSKNKDLSTP 445

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1280409835 142 VHYAV-NSENLSVVAKLLSCGADIEVKNKAGHTPLLLAIRKRSeeIVEFLL 191
Cdd:PHA02876  446 LHYACkKNCKLDVIEMLLDNGADVNAINIQNQYPLLIALEYHG--IVNILL 494
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 45-203 1.15e-06

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: 49.24  E-value: 1.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835  45 AASRGQAWKLERMMKKTTMDLNIRDAKKRTALYWACANGHAEVVTLLVDrkcqldvldgenrtilmkalqcqreaCANIL 124
Cdd:cd22192    24 AAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--------------------------AAPEL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835 125 IDsgaDPNIVDVY-GNTAVHYAVNSENLSVVAKLLSCGADIeVKNKA---------------GHTPLLLAIRKRSEEIVE 188
Cdd:cd22192    78 VN---EPMTSDLYqGETALHIAVVNQNLNLVRELIARGADV-VSPRAtgtffrpgpknliyyGEHPLSFAACVGNEEIVR 153

                         170
                  ....*....|....*
gi 1280409835 189 FLLTKNANANAVDKF 203
Cdd:cd22192   154 LLIEHGADIRAQDSL 168
Ank_4 pfam13637
Ankyrin repeats (many copies);
105-158 1.99e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.80  E-value: 1.99e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1280409835 105 NRTILMKALQCQREACANILIDSGADPNIVDVYGNTAVHYAVNSENLSVVAKLL 158
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 121-257 3.79e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 47.75  E-value: 3.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835 121 ANILIDSGADPNIVDVYGNTAVHYAVNSENLSVVAKLLSCGADIEVKNKAGHTPLLLAIRKRSEEIVEFLLTK--NANAN 198
Cdd:PHA02876  161 AEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNrsNINKN 240

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1280409835 199 AVDKFKCVHQQLLEYKQKISKNSQNSNPEGTSEGTPDEAAPLAERTPDTAESLVERTPD 257
Cdd:PHA02876  241 DLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLVPKLLERGAD 299
Ank_5 pfam13857
Ankyrin repeats (many copies);
90-145 1.27e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 1.27e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1280409835  90 LLVDRKCQLDVLDGENRTILMKALQCQREACANILIDSGADPNIVDVYGNTAVHYA 145
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 29-225 1.92e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 45.34  E-value: 1.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835  29 NDSYVIHhgdlrkihkAASRGQAWKLERMMKKTTMDLNIRDAKKRTALYWACANGHAEVVTLLVDRKCQLDVLDGENRTI 108
Cdd:PHA02874  156 NGCYPIH---------IAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTP 226

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835 109 LMKALQCQREACAniLIDSGADPNIVDVYGNTAVHYAVNSE-NLSVVAKLLSCGADIEVKNKAGHTPLLLAIRK-RSEEI 186
Cdd:PHA02874  227 LHNAIIHNRSAIE--LLINNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTAFKYiNKDPV 304

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1280409835 187 VEFLLTKNANANAVDKFKcvHQQLLEYKQkISKNSQNSN 225
Cdd:PHA02874  305 IKDIIANAVLIKEADKLK--DSDFLEHIE-IKDNKEFSD 340
PHA02791 PHA02791
ankyrin-like protein; Provisional
 47-193 2.69e-05

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 44.65  E-value: 2.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835  47 SRGQAWKLERMMK-KTTMDLNIRDAKKRTALYWACANGHAEVVTLLVDRKCQLDVLdgENRTILMKALQCQREACANILI 125
Cdd:PHA02791    4 SRINTWKSKQLKSfLSSKDAFKADVHGHSALYYAIADNNVRLVCTLLNAGALKNLL--ENEFPLHQAATLEDTKIVKILL 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1280409835 126 DSGADPNIVDVYGNTAVHYAVNSENLSVVAKLLSCGADIEVKNKAG-HTPLLLAIRKRSEEIVEFLLTK 193
Cdd:PHA02791   82 FSGMDDSQFDDKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTGwKTSFYHAVMLNDVSIVSYFLSE 150
Ank_4 pfam13637
Ankyrin repeats (many copies);
73-125 4.88e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.95  E-value: 4.88e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1280409835  73 RTALYWACANGHAEVVTLLVDRKCQLDVLDGENRTILMKALQCQREACANILI 125
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 106-230 7.21e-05

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: 43.59  E-value: 7.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835 106 RTILMKAL---QCQREACANILIDSGADPNIVDVY-----------GNTAVHYAVNSENLSVVAKLLSCGADIEVKNKA- 170
Cdd:cd22194    95 KTCLMKALlniNENTKEIVRILLAFAEENGILDRFinaeyteeayeGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGv 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835 171 -------------GHTPLLLAIRKRSEEIVEFLLTK----------------NANANAVDKFKCVHQQLLEYKQKISKNS 221
Cdd:cd22194   175 ffnpkykhegfyfGETPLALAACTNQPEIVQLLMEKestditsqdsrgntvlHALVTVAEDSKTQNDFVKRMYDMILLKS 254


                  ....*....
gi 1280409835 222 QNSNPEGTS 230
Cdd:cd22194   255 ENKNLETIR 263
Ank_5 pfam13857
Ankyrin repeats (many copies);
129-178 1.12e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.25  E-value: 1.12e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1280409835 129 ADPNIVDVYGNTAVHYAVNSENLSVVAKLLSCGADIEVKNKAGHTPLLLA 178
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
42-92 1.40e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.79  E-value: 1.40e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1280409835  42 IHKAASRGqawKLE--RMMKKTTMDLNIRDAKKRTALYWACANGHAEVVTLLV 92
Cdd:pfam13637   5 LHAAAASG---HLEllRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 53-204 2.13e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 42.36  E-value: 2.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835  53 KLERMMKKTTMDLNIRDAKKRTALYWACANGHAEVVtllvdrkcqldvldgenrtilmkalqcqreacaNILIDSGADPN 132
Cdd:PHA02876  159 LIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMV---------------------------------NLLLSYGADVN 205

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1280409835 133 IVDVYGNTAVHYAVNSENLSVVAKLLSCGADIEvKNKAGhtpLLLAIRKRSEEIVEFLLTKNANANAVDKFK 204
Cdd:PHA02876  206 IIALDDLSVLECAVDSKNIDTIKAIIDNRSNIN-KNDLS---LLKAIRNEDLETSLLLYDAGFSVNSIDDCK 273
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 137-169 2.50e-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: 37.65  E-value: 2.50e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1280409835 137 YGNTAVHYAVNSE-NLSVVAKLLSCGADIEVKNK 169
Cdd:pfam00023   1 DGNTPLHLAAGRRgNLEIVKLLLSKGADVNARDK 34
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 106-201 2.66e-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: 41.79  E-value: 2.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835 106 RTILMKA---LQCQREACANILIDSGAD----------PNIVDVY-GNTAVHYAVNSENLSVVAKLLSCGADIEVK---- 167
Cdd:cd21882    27 KTCLHKAalnLNDGVNEAIMLLLEAAPDsgnpkelvnaPCTDEFYqGQTALHIAIENRNLNLVRLLVENGADVSARatgr 106

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1280409835 168 --NKAGHT-------PLLLAIRKRSEEIVEFLLTKNANANAVD 201
Cdd:cd21882   107 ffRKSPGNlfyfgelPLSLAACTNQEEIVRLLLENGAQPAALE 149
Ank_5 pfam13857
Ankyrin repeats (many copies);
63-109 3.17e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.71  E-value: 3.17e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1280409835  63 MDLNIRDAKKRTALYWACANGHAEVVTLLVDRKCQLDVLDGENRTIL 109
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 56-160 3.52e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.42  E-value: 3.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835  56 RMMKKTTMDLNIRDAKKRTALYWACANGHAEVVTLlvdrkcqldvldgenrtilmkalqcqreacaniLIDSGADPNIVD 135
Cdd:PTZ00322   99 RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRV---------------------------------LLEFGADPTLLD 145

                          90       100
                  ....*....|....*....|....*
gi 1280409835 136 VYGNTAVHYAVNSENLSVVAKLLSC 160
Cdd:PTZ00322  146 KDGKTPLELAEENGFREVVQLLSRH 170
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 40-203 5.73e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 40.83  E-value: 5.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835  40 RKIHKAASRGQAWKLERMMKKTTMD-LNIRDAKKRTALYWACA-NGHAEVVTLLVDRKCQLDVLDgenrTILMKA-LQCQ 116
Cdd:TIGR00870  19 KAFLPAAERGDLASVYRDLEEPKKLnINCPDRLGRSALFVAAIeNENLELTELLLNLSCRGAVGD----TLLHAIsLEYV 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835 117 R--EACANILI----DSGADPNIVDVYGN------TAVHYAVNSENLSVVAKLLSCGADIEVKNKA-------------- 170
Cdd:TIGR00870  95 DavEAILLHLLaafrKSGPLELANDQYTSeftpgiTALHLAAHRQNYEIVKLLLERGASVPARACGdffvksqgvdsfyh 174

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1280409835 171 GHTPLLLAIRKRSEEIVEFLLTKNANANAVDKF 203
Cdd:TIGR00870 175 GESPLNAAACLGSPSIVALLSEDPADILTADSL 207
PHA02798 PHA02798
ankyrin-like protein; Provisional
 85-200 6.43e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 40.59  E-value: 6.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835  85 AEVVTLLVDRKCQLDVLDGENRTILMKALQC----QREACANIL--IDSGADPNIVDVYGNTAVHYAVNSENLSVVAKLL 158
Cdd:PHA02798  199 ADILKLFVDNGFIINKENKSHKKKFMEYLNSllydNKRFKKNILdfIFSYIDINQVDELGFNPLYYSVSHNNRKIFEYLL 278

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1280409835 159 SCGADIEVKNKAGHTPLLLAIRKRSEEIVEFLLTKNANANAV 200
Cdd:PHA02798  279 QLGGDINIITELGNTCLFTAFENESKFIFNSILNKKPNKNTI 320
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 171-202 6.56e-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: 6.56e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1280409835 171 GHTPLLLAIRKR-SEEIVEFLLTKNANANAVDK 202
Cdd:pfam00023   2 GNTPLHLAAGRRgNLEIVKLLLSKGADVNARDK 34
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 122-193 6.93e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 40.77  E-value: 6.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835 122 NILIDSGADPNIVDVYGNTAVHYAVNSENLSVVAK----LLSCGADIE------VKNKAGHTPLLLAIRKRSEEIVEFLL 191
Cdd:cd22192   153 RLLIEHGADIRAQDSLGNTVLHILVLQPNKTFACQmydlILSYDKEDDlqpldlVPNNQGLTPFKLAAKEGNIVMFQHLV 232


                  ..
gi 1280409835 192 TK 193
Cdd:cd22192   233 QK 234
PHA02917 PHA02917
ankyrin-like protein; Provisional
 115-231 7.28e-04

ankyrin-like protein; Provisional


Pssm-ID: 165231 [Multi-domain]  Cd Length: 661  Bit Score: 40.75  E-value: 7.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835 115 CQREACANILIDSGADPNIVDVYGNTAVHYAVNSENLSVVAKLLSCGADIEVKNKAGHTPLLLAIRK-RSEEIVEFLLTK 193
Cdd:PHA02917  429 CPILSTINICLPYLKDINMIDKRGETLLHKAVRYNKQSLVSLLLESGSDVNIRSNNGYTCIAIAINEsRNIELLKMLLCH 508

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1280409835 194 NAN-----------ANAVDKFKCVhQQLLEYKQKISKNSQNSNPEGTSE 231
Cdd:PHA02917  509 KPTldcvidslreiSNIVDNAYAI-KQCIKYAMIIDDCTSSKIPESISQ 556
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 42-200 7.33e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 40.43  E-value: 7.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835  42 IHKAASRGQAWKLERMMKKTTMDLNIRDAKKRTALYWAC--ANGHAEVVTLLVDrkCQLdVLDGENRTILMKALQCQrEA 119
Cdd:PHA02876   45 IHQALQLRQIDIVEEIIQQNPELIYITDHKCHSTLHTICiiPNVMDIVISLTLD--CDI-ILDIKYASIILNKHKLD-EA 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835 120 CANILIDSGADPNIVDVYGNTAVHYA------VNSENLSVVAKLLSCGADIEVKNKAGHTPLLLAIRKRSEEIVEFLLTK 193
Cdd:PHA02876  121 CIHILKEAISGNDIHYDKINESIEYMklikerIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSY 200


                  ....*..
gi 1280409835 194 NANANAV 200
Cdd:PHA02876  201 GADVNII 207
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 106-191 8.74e-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: 40.16  E-value: 8.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835 106 RTILMKA---LQCQREACANILIDSGADPNIV---------DVY--GNTAVHYAVNSENLSVVAKLLSCGADIEVKNKA- 170
Cdd:cd22193    30 KTCLMKAllnLNPGTNDTIRILLDIAEKTDNLkrfinaeytDEYyeGQTALHIAIERRQGDIVALLVENGADVHAHAKGr 109

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1280409835 171 -------------GHTPLLLAIRKRSEEIVEFLL 191
Cdd:cd22193   110 ffqpkyqgegfyfGELPLSLAACTNQPDIVQYLL 143
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 137-166 1.40e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.26  E-value: 1.40e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1280409835  137 YGNTAVHYAVNSENLSVVAKLLSCGADIEV 166
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 171-199 2.00e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.87  E-value: 2.00e-03
                           10        20
                   ....*....|....*....|....*....
gi 1280409835  171 GHTPLLLAIRKRSEEIVEFLLTKNANANA 199
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 171-199 2.13e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.93  E-value: 2.13e-03
                          10        20
                  ....*....|....*....|....*....
gi 1280409835 171 GHTPLLLAIRKRSEEIVEFLLTKNANANA 199
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 123-175 5.14e-03

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 37.97  E-value: 5.14e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1280409835 123 ILIDSGADPNIVDVYGNTAVHYAV--------------NSENLSVVAKLLSCGADIEVKNKAGHTPL 175
Cdd:PHA02716  337 LLHEYGNDLNEPDNIGNTVLHTYLsmlsvvnildpetdNDIRLDVIQCLISLGADITAVNCLGYTPL 403
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 73-100 5.57e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 33.72  E-value: 5.57e-03
                           10        20
                   ....*....|....*....|....*...
gi 1280409835   73 RTALYWACANGHAEVVTLLVDRKCQLDV 100
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
157-203 7.53e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 33.86  E-value: 7.53e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1280409835 157 LLSCG-ADIEVKNKAGHTPLLLAIRKRSEEIVEFLLTKNANANAVDKF 203
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEE 48
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 38-203 8.58e-03

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: 37.09  E-value: 8.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835  38 DLRKIHKAASRGQAWKLERMM------KKTTMDLNIRDAKK-RTALYWACANGHaevvtllvdrkcqldvlDGENRTILM 110
Cdd:cd22196     6 DRRRIFDAVAKGDCKELDGLLeylmrtKKRLTDSEFKDPETgKTCLLKAMLNLH-----------------NGQNDTISL 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280409835 111 KALQCQREACANILIDSGadpnIVDVY--GNTAVHYAVNSENLSVVAKLLSCGADIEV--------KNKA------GHTP 174
Cdd:cd22196    69 LLDIAEKTGNLKEFVNAA----YTDSYykGQTALHIAIERRNMHLVELLVQNGADVHArasgeffkKKKGgpgfyfGELP 144

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1280409835 175 LLLAIRKRSEEIVEFLLT---KNANANAVDKF 203
Cdd:cd22196   145 LSLAACTNQLDIVKFLLEnphSPADISARDSM 176
 
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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