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Conserved domains on  [gi|6322079|ref|NP_012154|]
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Hos4p [Saccharomyces cerevisiae S288C]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 11430360)

ankyrin repeat (ANK) domain-containing protein 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

CATH:  1.25.40.20
Gene Ontology:  GO:0005515
PubMed:  33435370|15152081|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];
325-435 2.43e-31

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 125.07  E-value: 2.43e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322079   325 YRDSGGRTRLQIACDKGKYDVVKKMIEEGGyDINDQDNAGNTALHEAALQGHIEIVELLIENGADVNIKSIEmfGDTPLI 404
Cdd:COG0666   82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDND--GNTPLH 158

                         90       100       110
                 ....*....|....*....|....*....|.
gi 6322079   405 DASANGHLDVVKYLLKNGADPTIRNAKGLTA 435
Cdd:COG0666  159 LAAANGNLEIVKLLLEAGADVNARDNDGETP 189
Ank_2 pfam12796
Ankyrin repeats (3 copies);
537-624 1.33e-10

Ankyrin repeats (3 copies);


:

Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.97  E-value: 1.33e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322079     537 LFKASKEGHLPYVGTYVENGGKIDLRSFFE------SVKCGHEDITSIFLAFgfpVNQTSRDNKTSALMVAVGRGHLGTV 610
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGrtalhlAAKNGHLEIVKLLLEH---ADVNLKDNGRTALHYAARSGHLEIV 77

                           90
                   ....*....|....
gi 6322079     611 KLLLEAGADPTKRD 624
Cdd:pfam12796   78 KLLLEKGADINVKD 91
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
325-435 2.43e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 125.07  E-value: 2.43e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322079   325 YRDSGGRTRLQIACDKGKYDVVKKMIEEGGyDINDQDNAGNTALHEAALQGHIEIVELLIENGADVNIKSIEmfGDTPLI 404
Cdd:COG0666   82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDND--GNTPLH 158

                         90       100       110
                 ....*....|....*....|....*....|.
gi 6322079   405 DASANGHLDVVKYLLKNGADPTIRNAKGLTA 435
Cdd:COG0666  159 LAAANGNLEIVKLLLEAGADVNARDNDGETP 189
Ank_2 pfam12796
Ankyrin repeats (3 copies);
334-429 1.11e-25

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 101.73  E-value: 1.11e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322079     334 LQIACDKGKYDVVKKMIEEGgYDINDQDNAGNTALHEAALQGHIEIVELLIENgADVNIKSiemFGDTPLIDASANGHLD 413
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD---NGRTALHYAARSGHLE 75

                           90
                   ....*....|....*.
gi 6322079     414 VVKYLLKNGADPTIRN 429
Cdd:pfam12796   76 IVKLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 327-434 3.54e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 69.69  E-value: 3.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322079    327 DSGGRTRLQIACDK--GKYDVVKKMIEEGGyDINDQDNAGNTALHEAALQGHI--EIVELLIENGADVNIK-SIEMF--- 398
Cdd:PHA03100  103 DNNGITPLLYAISKksNSYSIVEYLLDNGA-NVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKnRVNYLlsy 181

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 6322079    399 ----------GDTPLIDASANGHLDVVKYLLKNGADPTIRNAKGLT 434
Cdd:PHA03100  182 gvpinikdvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDT 227
Ank_2 pfam12796
Ankyrin repeats (3 copies);
537-624 1.33e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.97  E-value: 1.33e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322079     537 LFKASKEGHLPYVGTYVENGGKIDLRSFFE------SVKCGHEDITSIFLAFgfpVNQTSRDNKTSALMVAVGRGHLGTV 610
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGrtalhlAAKNGHLEIVKLLLEH---ADVNLKDNGRTALHYAARSGHLEIV 77

                           90
                   ....*....|....
gi 6322079     611 KLLLEAGADPTKRD 624
Cdd:pfam12796   78 KLLLEKGADINVKD 91
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 326-434 5.69e-09

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: 60.03  E-value: 5.69e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322079   326 RDSGGRTRLQIACDKGKYDVVKKMIEEGGYDIND----QDNAGNTALHEAALQGHIEIVELLIENGADV----------- 390
Cdd:cd22192   47 RGALGETALHVAALYDNLEAAVVLMEAAPELVNEpmtsDLYQGETALHIAVVNQNLNLVRELIARGADVvspratgtffr 126

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 6322079   391 -NIKSIEMFGDTPLIDASANGHLDVVKYLLKNGADPTIRNAKGLT 434
Cdd:cd22192  127 pGPKNLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNT 171
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 364-392 1.39e-07

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 48.35  E-value: 1.39e-07
                            10        20
                    ....*....|....*....|....*....
gi 6322079      364 GNTALHEAALQGHIEIVELLIENGADVNI 392
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
527-634 1.63e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 54.19  E-value: 1.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322079   527 DVTSRAGKEKLFKASKEGHLPYVGTYVENGGKIDLRSFFESVKCGHEDITSIFLAFGFPVNQTSRDNKTSALMVAVGRGH 606
Cdd:COG0666   20 LLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGD 99

                         90       100
                 ....*....|....*....|....*...
gi 6322079   607 LGTVKLLLEAGADPTKRDKKGRTALYYA 634
Cdd:COG0666  100 LEIVKLLLEAGADVNARDKDGETPLHLA 127
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 364-437 9.80e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 46.61  E-value: 9.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322079     364 GNTALHEAALQGHIEIVELLIENGADVNIK-------------SIEmFGDTPLIDASANGHLDVVKYLLKNGADPtirna 430
Cdd:TIGR00870  128 GITALHLAAHRQNYEIVKLLLERGASVPARacgdffvksqgvdSFY-HGESPLNAAACLGSPSIVALLSEDPADI----- 201


                   ....*..
gi 6322079     431 kgLTAFE 437
Cdd:TIGR00870  202 --LTADS 206
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 578-637 2.00e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.19  E-value: 2.00e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322079    578 IFLAFGFPVNQTSRDNKTsALMVAVGRGHLGTVKLLLEAGADPTKRDKKGRTALYYAKNS 637
Cdd:PTZ00322  100 ILLTGGADPNCRDYDGRT-PLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEEN 158
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
325-435 2.43e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 125.07  E-value: 2.43e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322079   325 YRDSGGRTRLQIACDKGKYDVVKKMIEEGGyDINDQDNAGNTALHEAALQGHIEIVELLIENGADVNIKSIEmfGDTPLI 404
Cdd:COG0666   82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDND--GNTPLH 158

                         90       100       110
                 ....*....|....*....|....*....|.
gi 6322079   405 DASANGHLDVVKYLLKNGADPTIRNAKGLTA 435
Cdd:COG0666  159 LAAANGNLEIVKLLLEAGADVNARDNDGETP 189
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
332-687 9.68e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 120.06  E-value: 9.68e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322079   332 TRLQIACDKGKYDVVKKMIEEGGYDINDQDNAGNTALHEAALQGHIEIVELLIENGADVNIKSIEmfGDTPLIDASANGH 411
Cdd:COG0666   55 ALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKD--GETPLHLAAYNGN 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322079   412 LDVVKYLLKNGADPTIRNAKGLTAfesvddesefddeedqkilreikkrLSIAAKKwtnragihndkskngnnahtidqp 491
Cdd:COG0666  133 LEIVKLLLEAGADVNAQDNDGNTP-------------------------LHLAAAN------------------------ 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322079   492 pfdnttkaknekaadspsmasnidekapeeefywtdvtsragkeklfkaskeghlpyvgtyvenggkidlrsffesvkcG 571
Cdd:COG0666  164 -------------------------------------------------------------------------------G 164

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322079   572 HEDITSIFLAFGFPVNQTSRDNKTsALMVAVGRGHLGTVKLLLEAGADPTKRDKKGRTALYYAKNsiMGITNSEEIQLIE 651
Cdd:COG0666  165 NLEIVKLLLEAGADVNARDNDGET-PLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAE--NGNLEIVKLLLEA 241

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 6322079   652 NAINNYLKKHSEDNNDDDDDDDNNNETYKHEKKREK 687
Cdd:COG0666  242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLL 277
Ank_2 pfam12796
Ankyrin repeats (3 copies);
334-429 1.11e-25

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 101.73  E-value: 1.11e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322079     334 LQIACDKGKYDVVKKMIEEGgYDINDQDNAGNTALHEAALQGHIEIVELLIENgADVNIKSiemFGDTPLIDASANGHLD 413
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD---NGRTALHYAARSGHLE 75

                           90
                   ....*....|....*.
gi 6322079     414 VVKYLLKNGADPTIRN 429
Cdd:pfam12796   76 IVKLLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
326-435 1.34e-25

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 108.12  E-value: 1.34e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322079   326 RDSGGRTRLQIACDKGKYDVVKKMIEEGGyDINDQDNAGNTALHEAALQGHIEIVELLIENGADVNIKSIEmfGDTPLID 405
Cdd:COG0666  149 QDNDGNTPLHLAAANGNLEIVKLLLEAGA-DVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDND--GKTALDL 225

                         90       100       110
                 ....*....|....*....|....*....|
gi 6322079   406 ASANGHLDVVKYLLKNGADPTIRNAKGLTA 435
Cdd:COG0666  226 AAENGNLEIVKLLLEAGADLNAKDKDGLTA 255
Ank_2 pfam12796
Ankyrin repeats (3 copies);
326-393 6.53e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.92  E-value: 6.53e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6322079     326 RDSGGRTRLQIACDKGKYDVVKKMIEEGgyDINDQDNaGNTALHEAALQGHIEIVELLIENGADVNIK 393
Cdd:pfam12796   26 QDKNGRTALHLAAKNGHLEIVKLLLEHA--DVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVK 90
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
326-436 1.60e-14

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 75.38  E-value: 1.60e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322079   326 RDSGGRTRLQIACDKGKYDVVKKMIEEGGyDINDQDNAGNTALHEAALQGHIEIVELLIENGADVNIKSIEmfGDTPLID 405
Cdd:COG0666  182 RDNDGETPLHLAAENGHLEIVKLLLEAGA-DVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKD--GLTALLL 258

                         90       100       110
                 ....*....|....*....|....*....|.
gi 6322079   406 ASANGHLDVVKYLLKNGADPTIRNAKGLTAF 436
Cdd:COG0666  259 AAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 327-434 3.54e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 69.69  E-value: 3.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322079    327 DSGGRTRLQIACDK--GKYDVVKKMIEEGGyDINDQDNAGNTALHEAALQGHI--EIVELLIENGADVNIK-SIEMF--- 398
Cdd:PHA03100  103 DNNGITPLLYAISKksNSYSIVEYLLDNGA-NVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKnRVNYLlsy 181

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 6322079    399 ----------GDTPLIDASANGHLDVVKYLLKNGADPTIRNAKGLT 434
Cdd:PHA03100  182 gvpinikdvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDT 227
Ank_4 pfam13637
Ankyrin repeats (many copies);
364-419 5.54e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 61.52  E-value: 5.54e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 6322079     364 GNTALHEAALQGHIEIVELLIENGADVNIKSIEmfGDTPLIDASANGHLDVVKYLL 419
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGN--GETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 344-438 8.79e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 65.43  E-value: 8.79e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322079    344 DVVKKMIEEGGyDINDQDNAGNTALHeAALQG---HIEIVELLIENGADVNikSIEMFGDTPLiDA---SANGHLDVVKY 417
Cdd:PHA03095   98 DVIKLLIKAGA-DVNAKDKVGRTPLH-VYLSGfniNPKVIRLLLRKGADVN--ALDLYGMTPL-AVllkSRNANVELLRL 172

                          90       100
                  ....*....|....*....|.
gi 6322079    418 LLKNGADPTIRNAKGLTAFES 438
Cdd:PHA03095  173 LIDAGADVYAVDDRFRSLLHH 193
Ank_4 pfam13637
Ankyrin repeats (many copies);
330-384 9.07e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.05  E-value: 9.07e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 6322079     330 GRTRLQIACDKGKYDVVKKMIEEGgYDINDQDNAGNTALHEAALQGHIEIVELLI 384
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKG-ADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
537-624 1.33e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.97  E-value: 1.33e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322079     537 LFKASKEGHLPYVGTYVENGGKIDLRSFFE------SVKCGHEDITSIFLAFgfpVNQTSRDNKTSALMVAVGRGHLGTV 610
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGrtalhlAAKNGHLEIVKLLLEH---ADVNLKDNGRTALHYAARSGHLEIV 77

                           90
                   ....*....|....
gi 6322079     611 KLLLEAGADPTKRD 624
Cdd:pfam12796   78 KLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 338-424 1.45e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 64.69  E-value: 1.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322079    338 CDKGKYDVVKKMIEEG---------------GYDINDQDNAGNTALHEAALQGHIEIVELLIENGADVNIKSieMFGDTP 402
Cdd:PHA03100  151 SNKIDLKILKLLIDKGvdinaknrvnyllsyGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVN--KYGDTP 228

                          90       100
                  ....*....|....*....|..
gi 6322079    403 LIDASANGHLDVVKYLLKNGAD 424
Cdd:PHA03100  229 LHIAILNNNKEIFKLLLNNGPS 250
PHA03095 PHA03095
ankyrin-like protein; Provisional
 325-435 1.92e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 64.66  E-value: 1.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322079    325 YRDSGGRTRL----QIACDKGKyDVVKKMIEEGGyDINDQDNAGNTALHEAALQGH-IEIVELLIENGADVNIKSIemFG 399
Cdd:PHA03095   42 FRGEYGKTPLhlylHYSSEKVK-DIVRLLLEAGA-DVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGADVNAKDK--VG 117

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 6322079    400 DTPL--IDASANGHLDVVKYLLKNGADPTIRNAKGLTA 435
Cdd:PHA03095  118 RTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTP 155
Ank_5 pfam13857
Ankyrin repeats (many copies);
349-403 1.08e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 55.05  E-value: 1.08e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 6322079     349 MIEEGGYDINDQDNAGNTALHEAALQGHIEIVELLIENGADVNIKsiEMFGDTPL 403
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLK--DEEGLTAL 53
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 326-434 3.65e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 60.36  E-value: 3.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322079    326 RDSGGRTRLQIACDKGKYDVVKKMIEEGGyDINDQDNAGNTALHEAALQGHIEIVELLIENGADVNIKsiEMFGDTPLID 405
Cdd:PHA02874  120 KDAELKTFLHYAIKKGDLESIKMLFEYGA-DVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVK--DNNGESPLHN 196

                          90       100
                  ....*....|....*....|....*....
gi 6322079    406 ASANGHLDVVKYLLKNGADPTIRNAKGLT 434
Cdd:PHA02874  197 AAEYGDYACIKLLIDHGNHIMNKCKNGFT 225
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 326-434 5.69e-09

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: 60.03  E-value: 5.69e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322079   326 RDSGGRTRLQIACDKGKYDVVKKMIEEGGYDIND----QDNAGNTALHEAALQGHIEIVELLIENGADV----------- 390
Cdd:cd22192   47 RGALGETALHVAALYDNLEAAVVLMEAAPELVNEpmtsDLYQGETALHIAVVNQNLNLVRELIARGADVvspratgtffr 126

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 6322079   391 -NIKSIEMFGDTPLIDASANGHLDVVKYLLKNGADPTIRNAKGLT 434
Cdd:cd22192  127 pGPKNLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNT 171
PHA03095 PHA03095
ankyrin-like protein; Provisional
 336-435 6.08e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 59.65  E-value: 6.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322079    336 IACDKGKYDVVKKMIEEGGyDINDQDNAGNTALH---EAALQGHIEIVELLIENGADVNIKSIemFGDTPLID-ASANGH 411
Cdd:PHA03095   20 LNASNVTVEEVRRLLAAGA-DVNFRGEYGKTPLHlylHYSSEKVKDIVRLLLEAGADVNAPER--CGFTPLHLyLYNATT 96

                          90       100
                  ....*....|....*....|....
gi 6322079    412 LDVVKYLLKNGADPTIRNAKGLTA 435
Cdd:PHA03095   97 LDVIKLLIKAGADVNAKDKVGRTP 120
Ank_5 pfam13857
Ankyrin repeats (many copies);
383-437 6.86e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 52.73  E-value: 6.86e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 6322079     383 LIENGaDVNIKSIEMFGDTPLIDASANGHLDVVKYLLKNGADPTIRNAKGLTAFE 437
Cdd:pfam13857    1 LLEHG-PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 324-436 8.17e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 59.27  E-value: 8.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322079    324 IYRDSGGRTRLQIACD--KGKYDVVKKMIEEGGyDINDQDNAGNTALHEAALQGHIE--IVELLIENGADVNIKSieMFG 399
Cdd:PHA03095  181 YAVDDRFRSLLHHHLQsfKPRARIVRELIRAGC-DPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARN--RYG 257

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 6322079    400 DTPLIDASANGHLDVVKYLLKNGADPTIRNAKGLTAF 436
Cdd:PHA03095  258 QTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 364-393 1.49e-08

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: 51.14  E-value: 1.49e-08
                           10        20        30
                   ....*....|....*....|....*....|.
gi 6322079     364 GNTALHEAALQ-GHIEIVELLIENGADVNIK 393
Cdd:pfam00023    2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNAR 32
Ank_2 pfam12796
Ankyrin repeats (3 copies);
564-659 5.74e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 51.27  E-value: 5.74e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322079     564 FFESVKCGHEDITSIFLAFGFPVNQTSRDNKTsALMVAVGRGHLGTVKLLLEAGAdpTKRDKKGRTALYYAknsimGITN 643
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRT-ALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYA-----ARSG 72

                           90
                   ....*....|....*...
gi 6322079     644 SEEI--QLIENAINNYLK 659
Cdd:pfam12796   73 HLEIvkLLLEKGADINVK 90
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 364-392 1.39e-07

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 48.35  E-value: 1.39e-07
                            10        20
                    ....*....|....*....|....*....
gi 6322079      364 GNTALHEAALQGHIEIVELLIENGADVNI 392
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
527-634 1.63e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 54.19  E-value: 1.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322079   527 DVTSRAGKEKLFKASKEGHLPYVGTYVENGGKIDLRSFFESVKCGHEDITSIFLAFGFPVNQTSRDNKTSALMVAVGRGH 606
Cdd:COG0666   20 LLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGD 99

                         90       100
                 ....*....|....*....|....*...
gi 6322079   607 LGTVKLLLEAGADPTKRDKKGRTALYYA 634
Cdd:COG0666  100 LEIVKLLLEAGADVNARDKDGETPLHLA 127
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 327-424 1.66e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 55.64  E-value: 1.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322079    327 DSGGRTRLQIACDKGKYDVVKKMIEEGgYDINDQDNAGNTALHEAALQGHIEIVELL-----IEN---GADV-------- 390
Cdd:PLN03192  555 DSKGRTPLHIAASKGYEDCVLVLLKHA-CNVHIRDANGNTALWNAISAKHHKIFRILyhfasISDphaAGDLlctaakrn 633

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 6322079    391 -------------NIKSIEMFGDTPLIDASANGHLDVVKYLLKNGAD 424
Cdd:PLN03192  634 dltamkellkqglNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGAD 680
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 334-425 1.79e-07

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 55.25  E-value: 1.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322079   334 LQIACDKGKYdvvKKMIEEGgydINDQDNAGNTALHEAALQGHIEIVELLIENGADVNIKSIE-----------MFGDTP 402
Cdd:cd22197   70 LEIDKDSGNP---KPLVNAQ---CTDEYYRGHSALHIAIEKRSLQCVKLLVENGADVHARACGrffqkkqgtcfYFGELP 143

                         90       100
                 ....*....|....*....|...
gi 6322079   403 LIDASANGHLDVVKYLLKNGADP 425
Cdd:cd22197  144 LSLAACTKQWDVVNYLLENPHQP 166
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 364-392 2.34e-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: 47.64  E-value: 2.34e-07
                           10        20
                   ....*....|....*....|....*....
gi 6322079     364 GNTALHEAALQGHIEIVELLIENGADVNI 392
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 344-437 4.12e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 53.52  E-value: 4.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322079    344 DVVKKMIEEGgYDINDQDNAGNTALHEAALQGHI-----EIVELLIENGADVNikSIEMFGDTPLIDASAN--GHLDVVK 416
Cdd:PHA03100   49 DVVKILLDNG-ADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVN--APDNNGITPLLYAISKksNSYSIVE 125

                          90       100
                  ....*....|....*....|.
gi 6322079    417 YLLKNGADPTIRNAKGLTAFE 437
Cdd:PHA03100  126 YLLDNGANVNIKNSDGENLLH 146
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 348-420 4.81e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.75  E-value: 4.81e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6322079    348 KMIEEGGYDINDQDNAGNTALHEAALQGHIEIVELLIENGADVNIKSIEmfGDTPLIDASANGHLDVVKYLLK 420
Cdd:PTZ00322   99 RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKD--GKTPLELAEENGFREVVQLLSR 169
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 348-434 5.84e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.43  E-value: 5.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322079    348 KMIEEGGYDINDQDNAGNTALHEAALQGHIEIVELLIENGADVNIKSIEmfGDTPLIDASANGHLDVVKYLLKNGADPTI 427
Cdd:PHA02874  108 KTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDN--GCYPIHIAIKHNFFDIIKLLLEKGAYANV 185


                  ....*..
gi 6322079    428 RNAKGLT 434
Cdd:PHA02874  186 KDNNGES 192
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 364-425 9.10e-07

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: 52.96  E-value: 9.10e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6322079   364 GNTALHEAALQGHIEIVELLIENGADVNIKS-----------IEMFGDTPLIDASANGHLDVVKYLLKNGADP 425
Cdd:cd21882   73 GQTALHIAIENRNLNLVRLLVENGADVSARAtgrffrkspgnLFYFGELPLSLAACTNQEEIVRLLLENGAQP 145
Ank_4 pfam13637
Ankyrin repeats (many copies);
595-634 9.66e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.50  E-value: 9.66e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 6322079     595 TSALMVAVGRGHLGTVKLLLEAGADPTKRDKKGRTALYYA 634
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFA 41
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 320-437 1.16e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.59  E-value: 1.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322079    320 QKKGIYRDSGGRTRLQIACDKgkydvvKKMIEEGGYDINDQ-------DNAGNTALHEAALQ-------GHIEIVEL--- 382
Cdd:PTZ00322   16 QLFFGTEGSRKRRAKPISFER------MAAIQEEIARIDTHlealeatENKDATPDHNLTTEevidpvvAHMLTVELcql 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6322079    383 -----------LIENGADVNikSIEMFGDTPLIDASANGHLDVVKYLLKNGADPTIRNAKGLTAFE 437
Cdd:PTZ00322   90 aasgdavgariLLTGGADPN--CRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLE 153
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 327-439 1.60e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 51.80  E-value: 1.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322079    327 DSGGRTRLQIACDKGKYDVVKKMIEEGGYdINDQDNAGNTALHEAALQ-GHIEIVELLIENGADVNIKSiEMFGDTPLid 405
Cdd:PHA02878  198 DKTNNSPLHHAVKHYNKPIVHILLENGAS-TDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKS-YILGLTAL-- 273

                          90       100       110
                  ....*....|....*....|....*....|....
gi 6322079    406 ASANGHLDVVKYLLKNGADPTIRNAKGLTAFESV 439
Cdd:PHA02878  274 HSSIKSERKLKLLLEYGADINSLNSYKLTPLSSA 307
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 332-425 2.05e-06

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: 52.07  E-value: 2.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322079   332 TRLQIACDKGKyDVVKKMI----EEGGYDindqdnaGNTALHEAALQGHIEIVELLIENGADVNIKSIEM---------- 397
Cdd:cd22194  113 VRILLAFAEEN-GILDRFInaeyTEEAYE-------GQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVffnpkykheg 184

                         90       100       110
                 ....*....|....*....|....*....|
gi 6322079   398 --FGDTPLIDASANGHLDVVKYLLKNGADP 425
Cdd:cd22194  185 fyFGETPLALAACTNQPEIVQLLMEKESTD 214
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 324-425 2.25e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 51.15  E-value: 2.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322079    324 IYRDsgGRTRLQIACDKGKYDVVKKMIEEGG-YDINDQDNAgnTALHEAALQGHIEIVELLIENGADVNIKsiEMFGDTP 402
Cdd:PHA02875   98 FYKD--GMTPLHLATILKKLDIMKLLIARGAdPDIPNTDKF--SPLHLAVMMGDIKGIELLIDHKACLDIE--DCCGCTP 171

                          90       100
                  ....*....|....*....|...
gi 6322079    403 LIDASANGHLDVVKYLLKNGADP 425
Cdd:PHA02875  172 LIIAMAKGDIAICKMLLDSGANI 194
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 399-429 2.87e-06

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. 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: 44.59  E-value: 2.87e-06
                           10        20        30
                   ....*....|....*....|....*....|..
gi 6322079     399 GDTPLIDASA-NGHLDVVKYLLKNGADPTIRN 429
Cdd:pfam00023    2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
PHA02798 PHA02798
ankyrin-like protein; Provisional
 342-437 2.95e-06

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 50.99  E-value: 2.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322079    342 KYDVVKKMIEEGGyDINDQDNAGNTAL-----HEAALQGHIEIVELLIENGADVNIKSIEmfGDTPLIDASANGH---LD 413
Cdd:PHA02798   50 STDIVKLFINLGA-NVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSD--GETPLYCLLSNGYinnLE 126

                          90       100
                  ....*....|....*....|....
gi 6322079    414 VVKYLLKNGADPTIRNAKGLTAFE 437
Cdd:PHA02798  127 ILLFMIENGADTTLLDKDGFTMLQ 150
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 337-424 4.72e-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: 50.78  E-value: 4.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322079   337 ACDKGKYDVVKKMIEEGGYDINDQDNAGNTALHEAALQGHIEIVELLIENGAD-VN--IKSiEMF-GDTPLIDASANGHL 412
Cdd:cd22192   24 AAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNepMTS-DLYqGETALHIAVVNQNL 102

                         90
                 ....*....|..
gi 6322079   413 DVVKYLLKNGAD 424
Cdd:cd22192  103 NLVRELIARGAD 114
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 364-434 6.54e-06

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: 50.18  E-value: 6.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322079   364 GNTALHEAALQGHIEIVELLIENGADVNIKSIEM------------FGDTPLIDASANGHLDVVKYLLKNG---ADPTIR 428
Cdd:cd22193   76 GQTALHIAIERRQGDIVALLVENGADVHAHAKGRffqpkyqgegfyFGELPLSLAACTNQPDIVQYLLENEhqpADIEAQ 155


                 ....*.
gi 6322079   429 NAKGLT 434
Cdd:cd22193  156 DSRGNT 161
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 330-438 8.32e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 49.49  E-value: 8.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322079    330 GRTRLQIACDKGKYDVVKKMIEEGGyDINDQDNAGNTALHEAALQGHIEIVELLIENGADVNIKSieMFGDTPL-IDASA 408
Cdd:PHA02878  168 GNTALHYATENKDQRLTELLLSYGA-NVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARD--KCGNTPLhISVGY 244

                          90       100       110
                  ....*....|....*....|....*....|.
gi 6322079    409 NGHLDVVKYLLKNGADPTIRNA-KGLTAFES 438
Cdd:PHA02878  245 CKDYDILKLLLEHGVDVNAKSYiLGLTALHS 275
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 399-427 1.00e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.96  E-value: 1.00e-05
                            10        20
                    ....*....|....*....|....*....
gi 6322079      399 GDTPLIDASANGHLDVVKYLLKNGADPTI 427
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
399-436 1.08e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.80  E-value: 1.08e-05
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 6322079     399 GDTPLIDASANGHLDVVKYLLKNGADPTIRNAKGLTAF 436
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETAL 38
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 339-434 1.55e-05

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: 49.03  E-value: 1.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322079   339 DKGKYDVVKKMIE--EGGYDINDQDNA--------GNTALHEAALQGHIEIVELLIENGADVNIKSIEM----------- 397
Cdd:cd22196   59 HNGQNDTISLLLDiaEKTGNLKEFVNAaytdsyykGQTALHIAIERRNMHLVELLVQNGADVHARASGEffkkkkggpgf 138

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 6322079   398 -FGDTPLIDASANGHLDVVKYLLKN---GADPTIRNAKGLT 434
Cdd:cd22196  139 yFGELPLSLAACTNQLDIVKFLLENphsPADISARDSMGNT 179
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 338-434 1.70e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 48.72  E-value: 1.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322079    338 CDKGKYDVVK----KMIEEGGYDINDQD-NAGNTALHEAALQGHIEIVELLIENGADVNIKSIEmfGDTPLIDASANGHL 412
Cdd:PHA02878  137 DKKSKDDIIEaeitKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKT--NNSPLHHAVKHYNK 214

                          90       100
                  ....*....|....*....|..
gi 6322079    413 DVVKYLLKNGADPTIRNAKGLT 434
Cdd:PHA02878  215 PIVHILLENGASTDARDKCGNT 236
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 326-432 1.91e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 48.42  E-value: 1.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322079    326 RDSGGRTRLQIACDKGKYDVVKKMIEEGGYdINDQDNAGNTALHEAALQGHIEIVELLIENGADVNIKSIEmfGDTPL-- 403
Cdd:PHA02874  153 EDDNGCYPIHIAIKHNFFDIIKLLLEKGAY-ANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKN--GFTPLhn 229

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 6322079    404 ----------------------IDASANGH--------LDVVKYLLKNGADPTIRNAKG 432
Cdd:PHA02874  230 aiihnrsaiellinnasindqdIDGSTPLHhainppcdIDIIDILLYHKADISIKDNKG 288
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 344-438 3.54e-05

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 47.98  E-value: 3.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322079    344 DVVKKMIEEGgYDINDQDNAGNTALHEAALQGHI--EIVELLIENGADVNikSIEMFGDTPL------------IDASAN 409
Cdd:PHA02716  298 SVVYSFLQPG-VKLHYKDSAGRTCLHQYILRHNIstDIIKLLHEYGNDLN--EPDNIGNTVLhtylsmlsvvniLDPETD 374

                          90       100       110
                  ....*....|....*....|....*....|.
gi 6322079    410 G--HLDVVKYLLKNGADPTIRNAKGLTAFES 438
Cdd:PHA02716  375 NdiRLDVIQCLISLGADITAVNCLGYTPLTS 405
Ank_2 pfam12796
Ankyrin repeats (3 copies);
403-435 5.76e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 42.80  E-value: 5.76e-05
                           10        20        30
                   ....*....|....*....|....*....|...
gi 6322079     403 LIDASANGHLDVVKYLLKNGADPTIRNAKGLTA 435
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTA 33
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 325-403 5.81e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 46.97  E-value: 5.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322079    325 YRDSGGRTRLQIACDKGKYDVVKKMIEEGGyDINDQDNAGNTALHEAALQGHIEIVELLIENGADVN--IKSIEMFGDTP 402
Cdd:PHA03100  187 IKDVYGFTPLHYAVYNNNPEFVKYLLDLGA-NPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKtiIETLLYFKDKD 265


                  .
gi 6322079    403 L 403
Cdd:PHA03100  266 L 266
Ank_5 pfam13857
Ankyrin repeats (many copies);
580-634 6.59e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.56  E-value: 6.59e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 6322079     580 LAFGFPVNQTSRDNKTSALMVAVGRGHLGTVKLLLEAGADPTKRDKKGRTALYYA 634
Cdd:pfam13857    2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 364-437 9.80e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 46.61  E-value: 9.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322079     364 GNTALHEAALQGHIEIVELLIENGADVNIK-------------SIEmFGDTPLIDASANGHLDVVKYLLKNGADPtirna 430
Cdd:TIGR00870  128 GITALHLAAHRQNYEIVKLLLERGASVPARacgdffvksqgvdSFY-HGESPLNAAACLGSPSIVALLSEDPADI----- 201


                   ....*..
gi 6322079     431 kgLTAFE 437
Cdd:TIGR00870  202 --LTADS 206
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 596-625 9.81e-05

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. 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: 40.35  E-value: 9.81e-05
                           10        20        30
                   ....*....|....*....|....*....|.
gi 6322079     596 SALMVAVGR-GHLGTVKLLLEAGADPTKRDK 625
Cdd:pfam00023    4 TPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 346-421 1.97e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.44  E-value: 1.97e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6322079    346 VKKMIEEGGYDINDQDNAGNTALHEAALQGHIEIVELLIENGADVNIksIEMFGDTPLIDASANGHLDVVKYLLKN 421
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNI--IALDDLSVLECAVDSKNIDTIKAIIDN 233
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 325-434 2.26e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 44.98  E-value: 2.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322079    325 YRDSGGRTRLQIACDKGKYDVVKKMIEEGGYdINDQ-DNAGNTALHEAALQGHIEIVELLIENGADVNIKSIEMFgdTPL 403
Cdd:PHA02875   63 VKYPDIESELHDAVEEGDVKAVEELLDLGKF-ADDVfYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKF--SPL 139

                          90       100       110
                  ....*....|....*....|....*....|.
gi 6322079    404 IDASANGHLDVVKYLLKNGADPTIRNAKGLT 434
Cdd:PHA02875  140 HLAVMMGDIKGIELLIDHKACLDIEDCCGCT 170
PHA02741 PHA02741
hypothetical protein; Provisional
 355-469 3.20e-04

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 42.72  E-value: 3.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322079    355 YDINDQDNAGNTALHEAAL----QGHIEIVELLIENGADVNIKSIeMFGDTPLIDASANGHLDVVKYLLKN-GADPTIRN 429
Cdd:PHA02741   51 AALNATDDAGQMCIHIAAEkheaQLAAEIIDHLIELGADINAQEM-LEGDTALHLAAHRRDHDLAEWLCCQpGIDLHFCN 129

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 6322079    430 AKGLTAFEsvdDESEFDDEEDQKILREIKKRLSIAAKKWT 469
Cdd:PHA02741  130 ADNKSPFE---LAIDNEDVAMMQILREIVATSRGFSNENT 166
PHA02798 PHA02798
ankyrin-like protein; Provisional
 340-431 4.59e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 44.06  E-value: 4.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322079    340 KGKYDVVKKMIEEGGyDINDQDNAGNTALHEAALQGHI---EIVELLIENGADVNIksIEMFGDTPL---IDASANGHLD 413
Cdd:PHA02798   86 KHMLDIVKILIENGA-DINKKNSDGETPLYCLLSNGYInnlEILLFMIENGADTTL--LDKDGFTMLqvyLQSNHHIDIE 162

                          90
                  ....*....|....*...
gi 6322079    414 VVKYLLKNGADPTIRNAK 431
Cdd:PHA02798  163 IIKLLLEKGVDINTHNNK 180
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 341-427 5.08e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 43.80  E-value: 5.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322079    341 GKYDVVKKMIEEGGYDINDQDNAGNTALHEAALQGHIEIVELLIENGADVNikSIEMFGDTPLIDASANGHLDVVKYLLK 420
Cdd:PHA02874   12 GDIEAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADIN--HINTKIPHPLLTAIKIGAHDIIKLLID 89


                  ....*..
gi 6322079    421 NGADPTI 427
Cdd:PHA02874   90 NGVDTSI 96
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 330-434 6.41e-04

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: 43.98  E-value: 6.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322079   330 GRTRLQIACDKGKYDVVKKMIEEGGyDIN-----------DQDNA---GNTALHEAALQGHIEIVELLIENGADvNIKSI 395
Cdd:cd22194  141 GQTALNIAIERRQGDIVKLLIAKGA-DVNahakgvffnpkYKHEGfyfGETPLALAACTNQPEIVQLLMEKEST-DITSQ 218

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 6322079   396 EMFGDT---PLIDASAN--GHLDVVKYLL-------KNGADPTIRNAKGLT 434
Cdd:cd22194  219 DSRGNTvlhALVTVAEDskTQNDFVKRMYdmillksENKNLETIRNNEGLT 269
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 349-424 9.12e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 43.13  E-value: 9.12e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6322079    349 MIEEGGYDINDQDNAGNTALHEAALQGHI-EIVELLIENGADVNIKSIEmfGDTPLIDASANGH-LDVVKYLLKNGAD 424
Cdd:PHA02876  258 LLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIK--GETPLYLMAKNGYdTENIRTLIMLGAD 333
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 334-390 1.27e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 42.93  E-value: 1.27e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 6322079    334 LQIACDKGKYDVVKKMIEEGgYDINDQDNAGNTALHEAALQGHIEIVELLIENGADV 390
Cdd:PLN03192  626 LCTAAKRNDLTAMKELLKQG-LNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 578-637 2.00e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.19  E-value: 2.00e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322079    578 IFLAFGFPVNQTSRDNKTsALMVAVGRGHLGTVKLLLEAGADPTKRDKKGRTALYYAKNS 637
Cdd:PTZ00322  100 ILLTGGADPNCRDYDGRT-PLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEEN 158
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 354-432 2.29e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 41.65  E-value: 2.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322079    354 GYDINDQDNaGNTALhEAALQGH---IEIVELLIENGADVNIKSiemFGDTPLIDASANGHLD------VVKYLLKNGAD 424
Cdd:PHA02989   26 GFDVNEEYR-GNSIL-LLYLKRKdvkIKIVKLLIDNGADVNYKG---YIETPLCAVLRNREITsnkikkIVKLLLKFGAD 100


                  ....*...
gi 6322079    425 PTIRNAKG 432
Cdd:PHA02989  101 INLKTFNG 108
Ank_5 pfam13857
Ankyrin repeats (many copies);
325-371 3.06e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.94  E-value: 3.06e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 6322079     325 YRDSGGRTRLQIACDKGKYDVVKKMIEEGGyDINDQDNAGNTALHEA 371
Cdd:pfam13857   11 RLDGEGYTPLHVAAKYGALEIVRVLLAYGV-DLNLKDEEGLTALDLA 56
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 368-437 3.75e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 41.20  E-value: 3.75e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322079    368 LHEAALQGHIEIVELLIENGADVNIKSIemFGDTPLIDASANGHLDVVKYLLKNGADPTIRNAKGLTAFE 437
Cdd:PHA02876  149 IKERIQQDELLIAEMLLEGGADVNAKDI--YCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLE 216
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 326-383 4.28e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.04  E-value: 4.28e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 6322079    326 RDSGGRTRLQIACDKGKYDVVKKMIEEGGyDINDQDNAGNTALHEAALQGHIEIVELL 383
Cdd:PTZ00322  111 RDYDGRTPLHIACANGHVQVVRVLLEFGA-DPTLLDKDGKTPLELAEENGFREVVQLL 167
 
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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