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Conserved domains on  [gi|148596917|ref|NP_660278|]
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fibronectin type 3 and ankyrin repeat domains protein 1 isoform 2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
114-341 4.56e-55

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 181.69  E-value: 4.56e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917 114 LHRAVSVNDEDLLVRILQGGRVKVDVPNKFGFTALMVAAQKGYTRLVKILVSNGTDVNLKNGSGKDSLMLACYAGHLDVV 193
Cdd:COG0666   57 LLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIV 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917 194 KYLRRHGASWQARDLGGCTALHWAADGGHCSVIEWMIKDGCEVDVVDtGSGWTPLMrVSAVSGNQRVASLLIDAGANVNV 273
Cdd:COG0666  137 KLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD-NDGETPLH-LAAENGHLEIVKLLLEAGADVNA 214

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148596917 274 KDRNGKTPLMVAVLNNHEELVQLLLDKGADASVKNEFGKGVLEMARVFDRQSVVSLLEERKKKQRPKK 341
Cdd:COG0666  215 KDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 9-93 6.65e-07

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


:

Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 46.45  E-value: 6.65e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917     9 PSKPHPPVVGKVTHHSIELYWdleKKAKRQGPQEQWFRFSIEEEDPKMHTYGIIYTGYATKHVVEGLEPRTLYRFRLKVT 88
Cdd:smart00060   1 PSPPSNLRVTDVTSTSVTLSW---EPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77


                   ....*
gi 148596917    89 SPSGE 93
Cdd:smart00060  78 NGAGE 82
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
114-341 4.56e-55

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 181.69  E-value: 4.56e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917 114 LHRAVSVNDEDLLVRILQGGRVKVDVPNKFGFTALMVAAQKGYTRLVKILVSNGTDVNLKNGSGKDSLMLACYAGHLDVV 193
Cdd:COG0666   57 LLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIV 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917 194 KYLRRHGASWQARDLGGCTALHWAADGGHCSVIEWMIKDGCEVDVVDtGSGWTPLMrVSAVSGNQRVASLLIDAGANVNV 273
Cdd:COG0666  137 KLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD-NDGETPLH-LAAENGHLEIVKLLLEAGADVNA 214

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148596917 274 KDRNGKTPLMVAVLNNHEELVQLLLDKGADASVKNEFGKGVLEMARVFDRQSVVSLLEERKKKQRPKK 341
Cdd:COG0666  215 KDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
Ank_2 pfam12796
Ankyrin repeats (3 copies);
148-240 1.98e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.49  E-value: 1.98e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917  148 LMVAAQKGYTRLVKILVSNGTDVNLKNGSGKDSLMLACYAGHLDVVKYLRRHGAswQARDLGGCTALHWAADGGHCSVIE 227
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 148596917  228 WMIKDGCEVDVVD 240
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 114-310 6.86e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 89.72  E-value: 6.86e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917 114 LHRAVSVNDEDLLVRILQGGrVKVDVPNKFGFTALMVAAQKGYT-----RLVKILVSNGTDVNlkNGSGKDSLMLACYA- 187
Cdd:PHA03100  39 LYLAKEARNIDVVKILLDNG-ADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVN--APDNNGITPLLYAIs 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917 188 ---GHLDVVKYLRRHGASWQARDLGGCTALHWAADGGH------------------CSVIEWMIKDGCEVDVVDTgSGWT 246
Cdd:PHA03100 116 kksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidlkilkllidkgvdinaKNRVNYLLSYGVPINIKDV-YGFT 194

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148596917 247 PLMrvSAV-SGNQRVASLLIDAGANVNVKDRNGKTPLMVAVLNNHEELVQLLLDKGADASVKNEF 310
Cdd:PHA03100 195 PLH--YAVyNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 9-93 6.65e-07

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 46.45  E-value: 6.65e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917     9 PSKPHPPVVGKVTHHSIELYWdleKKAKRQGPQEQWFRFSIEEEDPKMHTYGIIYTGYATKHVVEGLEPRTLYRFRLKVT 88
Cdd:smart00060   1 PSPPSNLRVTDVTSTSVTLSW---EPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77


                   ....*
gi 148596917    89 SPSGE 93
Cdd:smart00060  78 NGAGE 82
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 277-303 9.88e-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: 44.50  E-value: 9.88e-07
                           10        20
                   ....*....|....*....|....*..
gi 148596917   277 NGKTPLMVAVLNNHEELVQLLLDKGAD 303
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 146-299 2.03e-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: 2.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917 146 TALMVAAQKGYTRLVK-ILVSNGTDVNLKNGSGKDSLMLACYAGHLDVVKYLRRhgaswQARDL----------GGCTAL 214
Cdd:cd22192   19 SPLLLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME-----AAPELvnepmtsdlyQGETAL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917 215 HWAADGGHCSVIEWMIKDGceVDVVD---TGSGWTP-----------LMRVSAVSGNQRVASLLIDAGANVNVKDRNGKT 280
Cdd:cd22192   94 HIAVVNQNLNLVRELIARG--ADVVSpraTGTFFRPgpknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNT 171

                        170
                 ....*....|....*....
gi 148596917 281 PLMVAVLNNHEELVQLLLD 299
Cdd:cd22192  172 VLHILVLQPNKTFACQMYD 190
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 9-104 3.41e-06

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 44.79  E-value: 3.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917   9 PSKPHPPVVGKVTHHSIELYWDlekkaKRQGPQEQWFRFSIEEEDPKMHTYGIIYTGY--ATKHVVEGLEPRTLYRFRLK 86
Cdd:cd00063    1 PSPPTNLRVTDVTSTSVTLSWT-----PPEDDGGPITGYVVEYREKGSGDWKEVEVTPgsETSYTLTGLKPGTEYEFRVR 75

                         90
                 ....*....|....*...
gi 148596917  87 VTSPSGECEYSPLVSVST 104
Cdd:cd00063   76 AVNGGGESPPSESVTVTT 93
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 143-215 1.78e-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: 43.53  E-value: 1.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917  143 FGFTALMVAAQKGYTRLVKILVSNGTDVNLK-------NGSGKDSLM-----LACYA--GHLDVVKYLRRHGASWQARDL 208
Cdd:TIGR00870 127 PGITALHLAAHRQNYEIVKLLLERGASVPARacgdffvKSQGVDSFYhgespLNAAAclGSPSIVALLSEDPADILTADS 206


                  ....*..
gi 148596917  209 GGCTALH 215
Cdd:TIGR00870 207 LGNTLLH 213
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
114-341 4.56e-55

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 181.69  E-value: 4.56e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917 114 LHRAVSVNDEDLLVRILQGGRVKVDVPNKFGFTALMVAAQKGYTRLVKILVSNGTDVNLKNGSGKDSLMLACYAGHLDVV 193
Cdd:COG0666   57 LLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIV 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917 194 KYLRRHGASWQARDLGGCTALHWAADGGHCSVIEWMIKDGCEVDVVDtGSGWTPLMrVSAVSGNQRVASLLIDAGANVNV 273
Cdd:COG0666  137 KLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD-NDGETPLH-LAAENGHLEIVKLLLEAGADVNA 214

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148596917 274 KDRNGKTPLMVAVLNNHEELVQLLLDKGADASVKNEFGKGVLEMARVFDRQSVVSLLEERKKKQRPKK 341
Cdd:COG0666  215 KDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
113-340 1.59e-52

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 175.14  E-value: 1.59e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917 113 HLHRAVSVNDEDLLVRILQGGRVKVDVPNKFGFTALMVAAQKGYTRLVKILVSNGTDVNLKNGSGKDSLMLACYAGHLDV 192
Cdd:COG0666   23 LLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEI 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917 193 VKYLRRHGASWQARDLGGCTALHWAADGGHCSVIEWMIKDGCEVDVVDtGSGWTPLMrVSAVSGNQRVASLLIDAGANVN 272
Cdd:COG0666  103 VKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQD-NDGNTPLH-LAAANGNLEIVKLLLEAGADVN 180

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148596917 273 VKDRNGKTPLMVAVLNNHEELVQLLLDKGADASVKNEFGKGVLEMARVFDRQSVVSLLEERKKKQRPK 340
Cdd:COG0666  181 ARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAK 248
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
124-334 3.02e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 143.17  E-value: 3.02e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917 124 DLLVRILQGGRVKVDVPNKFGFTALMVAAQKGYTRLVKILVSNGTDVNLKNGSGKDSLMLACYAGHLDVVKYLRRHGASW 203
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917 204 QARDLGGCTALHWAADGGHCSVIEWMIKDGCEVDVVDTgSGWTPLMrVSAVSGNQRVASLLIDAGANVNVKDRNGKTPLM 283
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDK-DGETPLH-LAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLH 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 148596917 284 VAVLNNHEELVQLLLDKGADASVKNEFGKGVLEMARVFDRQSVVSLLEERK 334
Cdd:COG0666  159 LAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAG 209
Ank_2 pfam12796
Ankyrin repeats (3 copies);
148-240 1.98e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.49  E-value: 1.98e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917  148 LMVAAQKGYTRLVKILVSNGTDVNLKNGSGKDSLMLACYAGHLDVVKYLRRHGAswQARDLGGCTALHWAADGGHCSVIE 227
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 148596917  228 WMIKDGCEVDVVD 240
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
214-308 2.43e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.40  E-value: 2.43e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917  214 LHWAADGGHCSVIEWMIKDGCEVDVVDTgSGWTPLMrVSAVSGNQRVASLLIDaGANVNVKDrNGKTPLMVAVLNNHEEL 293
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDK-NGRTALH-LAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEI 76

                          90
                  ....*....|....*
gi 148596917  294 VQLLLDKGADASVKN 308
Cdd:pfam12796  77 VKLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 114-310 6.86e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 89.72  E-value: 6.86e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917 114 LHRAVSVNDEDLLVRILQGGrVKVDVPNKFGFTALMVAAQKGYT-----RLVKILVSNGTDVNlkNGSGKDSLMLACYA- 187
Cdd:PHA03100  39 LYLAKEARNIDVVKILLDNG-ADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVN--APDNNGITPLLYAIs 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917 188 ---GHLDVVKYLRRHGASWQARDLGGCTALHWAADGGH------------------CSVIEWMIKDGCEVDVVDTgSGWT 246
Cdd:PHA03100 116 kksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidlkilkllidkgvdinaKNRVNYLLSYGVPINIKDV-YGFT 194

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148596917 247 PLMrvSAV-SGNQRVASLLIDAGANVNVKDRNGKTPLMVAVLNNHEELVQLLLDKGADASVKNEF 310
Cdd:PHA03100 195 PLH--YAVyNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
Ank_2 pfam12796
Ankyrin repeats (3 copies);
114-207 3.61e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.93  E-value: 3.61e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917  114 LHRAVSVNDEDLLVRILQGGrVKVDVPNKFGFTALMVAAQKGYTRLVKILVSNGtDVNLKNgSGKDSLMLACYAGHLDVV 193
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKD-NGRTALHYAARSGHLEIV 77

                          90
                  ....*....|....
gi 148596917  194 KYLRRHGASWQARD 207
Cdd:pfam12796  78 KLLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 122-327 6.94e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 84.24  E-value: 6.94e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917 122 DEDLLVRILQGGrVKVDVPNKFGFTALMVAAQKGYTRLVKILVSNGTDVNLKNGSGKDSLMLACYAGHLDVVKYLRRHGA 201
Cdd:PHA02874 103 EKDMIKTILDCG-IDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGA 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917 202 SWQARDLGGCTALHWAADGGHCSVIEWMIKDGCEVdVVDTGSGWTPLMrvSAVSGNQRVASLLIDaGANVNVKDRNGKTP 281
Cdd:PHA02874 182 YANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHI-MNKCKNGFTPLH--NAIIHNRSAIELLIN-NASINDQDIDGSTP 257

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 148596917 282 LMVAV-LNNHEELVQLLLDKGADASVKNEFGKGVLEMA-RVFDRQSVV 327
Cdd:PHA02874 258 LHHAInPPCDIDIIDILLYHKADISIKDNKGENPIDTAfKYINKDPVI 305
PHA03095 PHA03095
ankyrin-like protein; Provisional
 124-306 9.31e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 77.76  E-value: 9.31e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917 124 DLLVRilQGGRVkvDVPNKFGFTALMVAAQKGYTR--LVKILVSNGTDVNLKNGSGKDSLmlACY--------------- 186
Cdd:PHA03095 101 KLLIK--AGADV--NAKDKVGRTPLHVYLSGFNINpkVIRLLLRKGADVNALDLYGMTPL--AVLlksrnanvellrlli 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917 187 -AG----------------HLD-------VVKYLRRHGASWQARDLGGCTALHWAADGGHC--SVIEWMIKDGCEVDVVD 240
Cdd:PHA03095 175 dAGadvyavddrfrsllhhHLQsfkprarIVRELIRAGCDPAATDMLGNTPLHSMATGSSCkrSLVLPLLIAGISINARN 254

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148596917 241 TgSGWTPLMrVSAVSGNQRVASLLIDAGANVNVKDRNGKTPLMVAVLNNHEELVQLLLDKGADASV 306
Cdd:PHA03095 255 R-YGQTPLH-YAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAET 318
PHA03095 PHA03095
ankyrin-like protein; Provisional
 121-333 2.17e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 73.91  E-value: 2.17e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917 121 NDEDLLVRILQGGRVKVDVpnkfgftalmvaaqkgytrlVKILVSNGTDVNLKNGSGKDSL-MLACYAGH--LDVVKYLR 197
Cdd:PHA03095  11 MEAALYDYLLNASNVTVEE--------------------VRRLLAAGADVNFRGEYGKTPLhLYLHYSSEkvKDIVRLLL 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917 198 RHGASWQARDLGGCTALH-WAADGGHCSVIEWMIKDGCEVDVVDtGSGWTPL-MRVSAVSGNQRVASLLIDAGANVNVKD 275
Cdd:PHA03095  71 EAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKD-KVGRTPLhVYLSGFNINPKVIRLLLRKGADVNALD 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148596917 276 RNGKTPLMVAVLNNH--EELVQLLLDKGADASVKNEFGKGVLE-MARVF-DRQSVVSLLEER 333
Cdd:PHA03095 150 LYGMTPLAVLLKSRNanVELLRLLIDAGADVYAVDDRFRSLLHhHLQSFkPRARIVRELIRA 211
PHA03095 PHA03095
ankyrin-like protein; Provisional
 137-324 5.77e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 72.36  E-value: 5.77e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917 137 VDVPNKFGFTALMVAAQKGYT-RLVKILVSNGTDVNLKNGSGKDSLMlACYAG---HLDVVKYLRRHGASWQARDLGGCT 212
Cdd:PHA03095  76 VNAPERCGFTPLHLYLYNATTlDVIKLLIKAGADVNAKDKVGRTPLH-VYLSGfniNPKVIRLLLRKGADVNALDLYGMT 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917 213 ALHWAADGGHCSV--IEWMIKDGCEVDVVDTgSGWTPL--MRVSAVSgNQRVASLLIDAGANVNVKDRNGKTPL--MVAV 286
Cdd:PHA03095 155 PLAVLLKSRNANVelLRLLIDAGADVYAVDD-RFRSLLhhHLQSFKP-RARIVRELIRAGCDPAATDMLGNTPLhsMATG 232

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 148596917 287 LNNHEELVQLLLDKGADASVKNEFGKGVLEMARVFDRQ 324
Cdd:PHA03095 233 SSCKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNP 270
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 114-308 1.45e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 71.63  E-value: 1.45e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917 114 LHRAVSVNDEDLLV-RILQGGrVKVDVPNKFGFTALMVAAQKGY-TRLVKILVSNGTDVNLKNGSGKDSLMLACYAG-HL 190
Cdd:PHA02876 277 LHHASQAPSLSRLVpKLLERG-ADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDrNK 355

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917 191 DVVKYLRRHGASWQARDLGGCTALHWAADGGHCSVIEWMIKDGCEVDVVDTGSGwTPLMrvSAVSGNQRVASL--LIDAG 268
Cdd:PHA02876 356 DIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIG-TALH--FALCGTNPYMSVktLIDRG 432

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 148596917 269 ANVNVKDRNGKTPLMVAVLNNHE-ELVQLLLDKGADASVKN 308
Cdd:PHA02876 433 ANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAIN 473
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 151-306 1.96e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 70.79  E-value: 1.96e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917 151 AAQKGYTRLVKILVSNGT---DVNLKNGSgkDSLMLACYAGHLDVVKYLRRHGASWQARDLGGCTALHWAADGGHCSVIE 227
Cdd:PHA02875  75 AVEEGDVKAVEELLDLGKfadDVFYKDGM--TPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIE 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917 228 WMIKDGCEVDVVDtGSGWTPLMrVSAVSGNQRVASLLIDAGANVNVKDRNGKTPLM-VAVLNNHEELVQLLLDKGADASV 306
Cdd:PHA02875 153 LLIDHKACLDIED-CCGCTPLI-IAMAKGDIAICKMLLDSGANIDYFGKNGCVAALcYAIENNKIDIVRLFIKRGADCNI 230
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 122-331 7.48e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 69.32  E-value: 7.48e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917 122 DEDLLVRILQGGRVKVDVPNKFGFTALMVAAQKGYTRLVKILVSNGTDVNLKNGSGKDSLMLACYAGHLDVVKYLRRHGA 201
Cdd:PHA02876 156 DELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRS 235

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917 202 SWQARDLGGCTALhwAADGGHCSVIewMIKDGCEVDVVDTGSGwTPLMRVSAVSGNQRVASLLIDAGANVNVKDRNGKTP 281
Cdd:PHA02876 236 NINKNDLSLLKAI--RNEDLETSLL--LYDAGFSVNSIDDCKN-TPLHHASQAPSLSRLVPKLLERGADVNAKNIKGETP 310

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 148596917 282 LMVAVLNNHE-ELVQLLLDKGADASVKNEFGKGVLEMARVFDR--QSVVSLLE 331
Cdd:PHA02876 311 LYLMAKNGYDtENIRTLIMLGADVNAADRLYITPLHQASTLDRnkDIVITLLE 363
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 123-287 7.59e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 66.06  E-value: 7.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917 123 EDLLVRIL--QGGRVKVDVPNKfGFTALMVAAQKGYTRLVKILVSNGTDVNLKNGSGKDSLMLACYAGHLDVVKYLRRHG 200
Cdd:PHA02878 146 EAEITKLLlsYGADINMKDRHK-GNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENG 224

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917 201 ASWQARDLGGCTALHWAAdgGHC---SVIEWMIKDGCEVDVVDTGSGWTPLMrvSAVSgNQRVASLLIDAGANVNVKDRN 277
Cdd:PHA02878 225 ASTDARDKCGNTPLHISV--GYCkdyDILKLLLEHGVDVNAKSYILGLTALH--SSIK-SERKLKLLLEYGADINSLNSY 299

                        170
                 ....*....|
gi 148596917 278 GKTPLMVAVL 287
Cdd:PHA02878 300 KLTPLSSAVK 309
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 146-330 1.25e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 65.37  E-value: 1.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917 146 TALMVAAQKGYTRLVKILVSNGTDVNLKNGSGKDSLMLACYAGHLDVVKYLRRHGASW---------------------- 203
Cdd:PHA02874  37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTsilpipciekdmiktildcgid 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917 204 -QARDLGGCTALHWAADGGHCSVIEWMIKDGCEVDVVDTgSGWTPLmRVSAVSGNQRVASLLIDAGANVNVKDRNGKTPL 282
Cdd:PHA02874 117 vNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDD-NGCYPI-HIAIKHNFFDIIKLLLEKGAYANVKDNNGESPL 194

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 148596917 283 MVAVLNNHEELVQLLLDKGADASVKNEFGKGVLEMARVFDRqSVVSLL 330
Cdd:PHA02874 195 HNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELL 241
Ank_2 pfam12796
Ankyrin repeats (3 copies);
248-330 3.05e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.97  E-value: 3.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917  248 LMrVSAVSGNQRVASLLIDAGANVNVKDRNGKTPLMVAVLNNHEELVQLLLDKgADASVKNEfGKGVLEMARVFDRQSVV 327
Cdd:pfam12796   1 LH-LAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIV 77


                  ...
gi 148596917  328 SLL 330
Cdd:pfam12796  78 KLL 80
Ank_4 pfam13637
Ankyrin repeats (many copies);
181-230 3.35e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 57.67  E-value: 3.35e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 148596917  181 LMLACYAGHLDVVKYLRRHGASWQARDLGGCTALHWAADGGHCSVIEWMI 230
Cdd:pfam13637   5 LHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 148-310 4.25e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 64.12  E-value: 4.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917 148 LMVAAQKGYTRLVKILVSNGTDVNLKNGSGKDSLMLACYAGHLDVVKYLRRHGASWQARDLGGCTALHWAADGGHCSvIE 227
Cdd:PLN03192 529 LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHK-IF 607

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917 228 WMIKDGCEVDVVDTGSGwtpLMRVSAVSGNQRVASLLIDAGANVNVKDRNGKTPLMVAVLNNHEELVQLLLDKGAD---A 304
Cdd:PLN03192 608 RILYHFASISDPHAAGD---LLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADvdkA 684


                 ....*.
gi 148596917 305 SVKNEF 310
Cdd:PLN03192 685 NTDDDF 690
Ank_5 pfam13857
Ankyrin repeats (many copies);
264-318 4.98e-10

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 54.66  E-value: 4.98e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 148596917  264 LIDAG-ANVNVKDRNGKTPLMVAVLNNHEELVQLLLDKGADASVKNEFGKGVLEMA 318
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 253-330 1.03e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 59.91  E-value: 1.03e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148596917 253 AVSGNQRVASLLIDAGANVNVKDRNGKTPLMVAVLNNHEELVQLLLDKGADASVKNEFGKGVLEMARVFDRQSVVSLL 330
Cdd:PTZ00322  90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
Ank_4 pfam13637
Ankyrin repeats (many copies);
244-298 4.29e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.89  E-value: 4.29e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 148596917  244 GWTPLMRVsAVSGNQRVASLLIDAGANVNVKDRNGKTPLMVAVLNNHEELVQLLL 298
Cdd:pfam13637   1 ELTALHAA-AASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
146-196 4.93e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.89  E-value: 4.93e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 148596917  146 TALMVAAQKGYTRLVKILVSNGTDVNLKNGSGKDSLMLACYAGHLDVVKYL 196
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 225-333 1.50e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 56.04  E-value: 1.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917 225 VIEWMIKDGCEVDVVDTGSGWTPLmRVSAVSGNQRVASLLIDAGANVNVKDRNGKTPLMVAVLNNHEELVQLLLDKGADA 304
Cdd:PHA02878 149 ITKLLLSYGADINMKDRHKGNTAL-HYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAST 227

                         90       100       110
                 ....*....|....*....|....*....|.
gi 148596917 305 SVKNEFGKGVLEMA--RVFDrQSVVSLLEER 333
Cdd:PHA02878 228 DARDKCGNTPLHISvgYCKD-YDILKLLLEH 257
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 107-248 1.56e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 56.03  E-value: 1.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917 107 EPISSEHLHRAVSVNDEDLLVRILQGGRvKVDVPNKFGFTALMVAAQKGYTRLVKILVSNGTDVNLKNGSGKDSLMLACY 186
Cdd:PLN03192 522 DPNMASNLLTVASTGNAALLEELLKAKL-DPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAIS 600

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917 187 AGH-------------------------------LDVVKYLRRHGASWQARDLGGCTALHWAADGGHCSVIEWMIKDGCE 235
Cdd:PLN03192 601 AKHhkifrilyhfasisdphaagdllctaakrndLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGAD 680

                        170
                 ....*....|...
gi 148596917 236 VDVVDTGSGWTPL 248
Cdd:PLN03192 681 VDKANTDDDFSPT 693
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
114-214 1.92e-08

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 54.96  E-value: 1.92e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917 114 LHRAVSVNDEDLlVRILQGGRVKVDVPNKFGFTALMVAAQKGYTRLVKILVSNGTDVNLKNGSGKDSLMLACYAGHLDVV 193
Cdd:COG0666  190 LHLAAENGHLEI-VKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIV 268

                         90       100
                 ....*....|....*....|.
gi 148596917 194 KYLRRHGASWQARDLGGCTAL 214
Cdd:COG0666  269 KLLLLALLLLAAALLDLLTLL 289
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 117-333 1.94e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 55.38  E-value: 1.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917 117 AVSVNDEDLLVRILQGG-RVKVDVPNkfGFTALMVAAQKGYTRLVKILVSNGTDVNLKNGSGKDSLMLACYAGHLDVVKY 195
Cdd:PHA02875   9 AILFGELDIARRLLDIGiNPNFEIYD--GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEE 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917 196 LRRHGASwqARDL---GGCTALHWAADGGHCSVIEWMIKDGCEVDVVDTGSgWTPLmRVSAVSGNQRVASLLIDAGANVN 272
Cdd:PHA02875  87 LLDLGKF--ADDVfykDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDK-FSPL-HLAVMMGDIKGIELLIDHKACLD 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148596917 273 VKDRNGKTPLMVAVLNNHEELVQLLLDKGADAsvkNEFGK----GVLEMARVFDRQSVVSLLEER 333
Cdd:PHA02875 163 IEDCCGCTPLIIAMAKGDIAICKMLLDSGANI---DYFGKngcvAALCYAIENNKIDIVRLFIKR 224
Ank_5 pfam13857
Ankyrin repeats (many copies);
163-217 7.69e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.50  E-value: 7.69e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 148596917  163 LVSNGT-DVNLKNGSGKDSLMLACYAGHLDVVKYLRRHGASWQARDLGGCTALHWA 217
Cdd:pfam13857   1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 9-93 6.65e-07

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 46.45  E-value: 6.65e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917     9 PSKPHPPVVGKVTHHSIELYWdleKKAKRQGPQEQWFRFSIEEEDPKMHTYGIIYTGYATKHVVEGLEPRTLYRFRLKVT 88
Cdd:smart00060   1 PSPPSNLRVTDVTSTSVTLSW---EPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77


                   ....*
gi 148596917    89 SPSGE 93
Cdd:smart00060  78 NGAGE 82
Ank_5 pfam13857
Ankyrin repeats (many copies);
129-184 8.85e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.42  E-value: 8.85e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 148596917  129 ILQGGRVKVDVPNKFGFTALMVAAQKGYTRLVKILVSNGTDVNLKNGSGKDSLMLA 184
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 277-303 9.88e-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: 44.50  E-value: 9.88e-07
                           10        20
                   ....*....|....*....|....*..
gi 148596917   277 NGKTPLMVAVLNNHEELVQLLLDKGAD 303
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 146-299 2.03e-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: 2.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917 146 TALMVAAQKGYTRLVK-ILVSNGTDVNLKNGSGKDSLMLACYAGHLDVVKYLRRhgaswQARDL----------GGCTAL 214
Cdd:cd22192   19 SPLLLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME-----AAPELvnepmtsdlyQGETAL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917 215 HWAADGGHCSVIEWMIKDGceVDVVD---TGSGWTP-----------LMRVSAVSGNQRVASLLIDAGANVNVKDRNGKT 280
Cdd:cd22192   94 HIAVVNQNLNLVRELIARG--ADVVSpraTGTFFRPgpknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNT 171

                        170
                 ....*....|....*....
gi 148596917 281 PLMVAVLNNHEELVQLLLD 299
Cdd:cd22192  172 VLHILVLQPNKTFACQMYD 190
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 229-298 2.23e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.51  E-value: 2.23e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917 229 MIKDGCEVDVVDTgSGWTPLmRVSAVSGNQRVASLLIDAGANVNVKDRNGKTPLMVAVLNNHEELVQLLL 298
Cdd:PTZ00322 101 LLTGGADPNCRDY-DGRTPL-HIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 9-104 3.41e-06

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 44.79  E-value: 3.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917   9 PSKPHPPVVGKVTHHSIELYWDlekkaKRQGPQEQWFRFSIEEEDPKMHTYGIIYTGY--ATKHVVEGLEPRTLYRFRLK 86
Cdd:cd00063    1 PSPPTNLRVTDVTSTSVTLSWT-----PPEDDGGPITGYVVEYREKGSGDWKEVEVTPgsETSYTLTGLKPGTEYEFRVR 75

                         90
                 ....*....|....*...
gi 148596917  87 VTSPSGECEYSPLVSVST 104
Cdd:cd00063   76 AVNGGGESPPSESVTVTT 93
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 277-309 4.19e-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: 43.05  E-value: 4.19e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 148596917  277 NGKTPLMVAVL-NNHEELVQLLLDKGADASVKNE 309
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
195-248 9.43e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 9.43e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 148596917  195 YLRRHGASWQARDLGGCTALHWAADGGHCSVIEWMIKDGCEVDVVDtGSGWTPL 248
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKD-EEGLTAL 53
PHA02798 PHA02798
ankyrin-like protein; Provisional
 159-318 1.04e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 47.14  E-value: 1.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917 159 LVKILVSNGTDVNLKNGSGKDSL--MLA-CYAGHLDVVKYLRRHGASWQARDLGGCTALHWAADGGH---CSVIEWMIKD 232
Cdd:PHA02798  91 IVKILIENGADINKKNSDGETPLycLLSnGYINNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEK 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917 233 GCEVDVVDTGSGWTPL---------------------------------------MRVSAVSGNQRVASLLID---AGAN 270
Cdd:PHA02798 171 GVDINTHNNKEKYDTLhcyfkynidridadilklfvdngfiinkenkshkkkfmeYLNSLLYDNKRFKKNILDfifSYID 250

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 148596917 271 VNVKDRNGKTPLMVAVLNNHEELVQLLLDKGADASVKNEFGKGVLEMA 318
Cdd:PHA02798 251 INQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTA 298
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 244-276 1.31e-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: 41.51  E-value: 1.31e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 148596917  244 GWTPLMRVSAVSGNQRVASLLIDAGANVNVKDR 276
Cdd:pfam00023   2 GNTPLHLAAGRRGNLEIVKLLLSKGADVNARDK 34
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 221-316 1.32e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 46.50  E-value: 1.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917 221 GHCSVIEWMIKDGCEVDVVDTGSGWTPLmrVSAV-SGNQRVASLLIDAGANVNVKDRNGKTPLMVAVLNNHEELVQLLLD 299
Cdd:PHA02874  12 GDIEAIEKIIKNKGNCINISVDETTTPL--IDAIrSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLID 89

                         90       100
                 ....*....|....*....|...
gi 148596917 300 KGADASV------KNEFGKGVLE 316
Cdd:PHA02874  90 NGVDTSIlpipciEKDMIKTILD 112
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 277-306 1.63e-05

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 41.09  E-value: 1.63e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 148596917  277 NGKTPLMVAVLNNHEELVQLLLDKGADASV 306
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02798 PHA02798
ankyrin-like protein; Provisional
 190-311 2.23e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 45.98  E-value: 2.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917 190 LDVVKYLRRHGASWQARD----LGGCTALHWAADGGH-CSVIEWMIKDGCEVDVVDTgSGWTPL--MRVSAVSGNQRVAS 262
Cdd:PHA02798  51 TDIVKLFINLGANVNGLDneysTPLCTILSNIKDYKHmLDIVKILIENGADINKKNS-DGETPLycLLSNGYINNLEILL 129

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 148596917 263 LLIDAGANVNVKDRNGKTPLMVAVLNNHE---ELVQLLLDKGADASV-KNEFG 311
Cdd:PHA02798 130 FMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDINThNNKEK 182
PHA02798 PHA02798
ankyrin-like protein; Provisional
 96-273 2.41e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 45.98  E-value: 2.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917  96 YSPLVSVSTTREPISSEHLHraVSVNDEDLLVRILQGGRVKVDVpnkfgftalmvaaqkgytrlVKILVSNGTDVNlkng 175
Cdd:PHA02798  12 FSDNVKLSTVKLLIKSCNPN--EIVNEYSIFQKYLQRDSPSTDI--------------------VKLFINLGANVN---- 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917 176 sGKDSLM----------LACYAGHLDVVKYLRRHGASWQARDLGGCTALHWAADGGHCSVIE---WMIKDGCEVDVVDtG 242
Cdd:PHA02798  66 -GLDNEYstplctilsnIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEillFMIENGADTTLLD-K 143

                        170       180       190
                 ....*....|....*....|....*....|....
gi 148596917 243 SGWTPLmRVSAVSGNQ---RVASLLIDAGANVNV 273
Cdd:PHA02798 144 DGFTML-QVYLQSNHHidiEIIKLLLEKGVDINT 176
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 144-174 3.49e-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: 3.49e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 148596917  144 GFTALMVAA-QKGYTRLVKILVSNGTDVNLKN 174
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 144-215 4.66e-05

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: 45.26  E-value: 4.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917 144 GFTALMVAAQKGYTRLVKILVSNGTDVNLK-NGS------------GKDSLMLACYAGHLDVVKYLRRHG---ASWQARD 207
Cdd:cd21882   73 GQTALHIAIENRNLNLVRLLVENGADVSARaTGRffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGaqpAALEAQD 152


                 ....*...
gi 148596917 208 LGGCTALH 215
Cdd:cd21882  153 SLGNTVLH 160
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 144-215 7.92e-05

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: 44.46  E-value: 7.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917 144 GFTALMVAAQKGYTRLVKILVSNGTDVNL---------KNGS----GKDSLMLACYAGHLDVVKYL---RRHGASWQARD 207
Cdd:cd22197   94 GHSALHIAIEKRSLQCVKLLVENGADVHAracgrffqkKQGTcfyfGELPLSLAACTKQWDVVNYLlenPHQPASLQAQD 173


                 ....*...
gi 148596917 208 LGGCTALH 215
Cdd:cd22197  174 SLGNTVLH 181
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 114-257 1.11e-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: 43.85  E-value: 1.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917 114 LHRAVSVNDEDLLVRILQGGRVKVDVPNK----FGFTALMVAAQKGYTRLVKILVSNGTDVNLKNGSG------KDSLML 183
Cdd:cd22192   55 LHVAALYDNLEAAVVLMEAAPELVNEPMTsdlyQGETALHIAVVNQNLNLVRELIARGADVVSPRATGtffrpgPKNLIY 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917 184 ---------ACyAGHLDVVKYLRRHGASWQARDLGGCTALH----WAADGGHCSVIEWMI-----KDGCEVDVVDTGSGW 245
Cdd:cd22192  135 ygehplsfaAC-VGNEEIVRLLIEHGADIRAQDSLGNTVLHilvlQPNKTFACQMYDLILsydkeDDLQPLDLVPNNQGL 213

                        170
                 ....*....|..
gi 148596917 246 TPlMRVSAVSGN 257
Cdd:cd22192  214 TP-FKLAAKEGN 224
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 259-315 1.64e-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: 43.59  E-value: 1.64e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148596917 259 RVASLLIDAGANVNV---------KDRN-----GKTPLMVAVLNNHEELVQLLLDKGAD-ASVKNEFGKGVL 315
Cdd:cd22194  155 DIVKLLIAKGADVNAhakgvffnpKYKHegfyfGETPLALAACTNQPEIVQLLMEKESTdITSQDSRGNTVL 226
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 143-215 1.78e-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: 43.53  E-value: 1.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917  143 FGFTALMVAAQKGYTRLVKILVSNGTDVNLK-------NGSGKDSLM-----LACYA--GHLDVVKYLRRHGASWQARDL 208
Cdd:TIGR00870 127 PGITALHLAAHRQNYEIVKLLLERGASVPARacgdffvKSQGVDSFYhgespLNAAAclGSPSIVALLSEDPADILTADS 206


                  ....*..
gi 148596917  209 GGCTALH 215
Cdd:TIGR00870 207 LGNTLLH 213
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 225-315 2.41e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 41.73  E-value: 2.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917 225 VIEWMIKDGCEVDVVDTGSGWTPLMRVSAVSGN--QRVASLLIDAGANVNVKDRNGKTPLMVAV--LNNHEELVQLLLDK 300
Cdd:PHA02859  68 ILKFLIENGADVNFKTRDNNLSALHHYLSFNKNvePEILKILIDSGSSITEEDEDGKNLLHMYMcnFNVRINVIKLLIDS 147

                         90
                 ....*....|....*
gi 148596917 301 GADASVKNEFGKGVL 315
Cdd:PHA02859 148 GVSFLNKDFDNNNIL 162
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 259-343 3.20e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 42.17  E-value: 3.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917 259 RVASLLIDAGANVNVKDRN-GKTPLMVAVLNNHEELVQLLLDKGADASVKNEFGKGVLEMARVFDRQSVVSLLEERKKKQ 337
Cdd:PHA02878 148 EITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAST 227


                 ....*.
gi 148596917 338 RPKKSC 343
Cdd:PHA02878 228 DARDKC 233
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 210-238 3.29e-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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.62  E-value: 3.29e-04
                          10        20
                  ....*....|....*....|....*....
gi 148596917  210 GCTALHWAADGGHCSVIEWMIKDGCEVDV 238
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 144-172 3.41e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.57  E-value: 3.41e-04
                           10        20
                   ....*....|....*....|....*....
gi 148596917   144 GFTALMVAAQKGYTRLVKILVSNGTDVNL 172
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 210-240 4.40e-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: 37.27  E-value: 4.40e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 148596917  210 GCTALHWAAD-GGHCSVIEWMIKDGCEVDVVD 240
Cdd:pfam00023   2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 152-227 4.85e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.81  E-value: 4.85e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148596917 152 AQKGYTRLVKILVSNGTDVNLKNGSGKDSLMLACYAGHLDVVKYLRRHGASWQARDLGGCTALHWAADGGHCSVIE 227
Cdd:PTZ00322  90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 212-303 5.10e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 41.92  E-value: 5.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917 212 TALHWAADGGHCSVIEWMIKdgCE-VDVVDTGS-GWTPLmRVSAVSGNQRVASLLIDAGAN-VNVKDRN----GKTPLMV 284
Cdd:cd22192   19 SPLLLAAKENDVQAIKKLLK--CPsCDLFQRGAlGETAL-HVAALYDNLEAAVVLMEAAPElVNEPMTSdlyqGETALHI 95

                         90
                 ....*....|....*....
gi 148596917 285 AVLNNHEELVQLLLDKGAD 303
Cdd:cd22192   96 AVVNQNLNLVRELIARGAD 114
PHA02795 PHA02795
ankyrin-like protein; Provisional
 129-242 8.54e-04

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 41.13  E-value: 8.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917 129 ILQGGRVKVDVPNKFGFTALMVAAQKGYTRLVKILVSNGTDVNLKNGSGKDSLMLACYAGHLDVVKYLRRHGASWQARDL 208
Cdd:PHA02795 173 IPDENDVKLDLYKIIQYTRGFLVDEPTVLEIYKLCIPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMS 252

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 148596917 209 GGCTALHWAADGG--------HCSVIEWMIKDGCEVDVVDTG 242
Cdd:PHA02795 253 NGYTCLDVAVDRGsviarretHLKILEILLREPLSIDCIKLA 294
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 191-317 9.09e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 41.15  E-value: 9.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917 191 DVVKYLRRHGASWQARDLGGCTALHWAADGGHCSVIEWMIKDGCE-VDVVDTGS---GWTPLmRVSAVSGNQRVASLLID 266
Cdd:cd22192   32 AIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPMTSDlyqGETAL-HIAVVNQNLNLVRELIA 110

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148596917 267 AGANVnVKDRN---------------GKTPLMVAVLNNHEELVQLLLDKGADASVKNEFGKGVLEM 317
Cdd:cd22192  111 RGADV-VSPRAtgtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175
Ank_4 pfam13637
Ankyrin repeats (many copies);
280-318 1.40e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.48  E-value: 1.40e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 148596917  280 TPLMVAVLNNHEELVQLLLDKGADASVKNEFGKGVLEMA 318
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFA 41
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 210-238 1.73e-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: 1.73e-03
                           10        20
                   ....*....|....*....|....*....
gi 148596917   210 GCTALHWAADGGHCSVIEWMIKDGCEVDV 238
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 257-317 2.24e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 38.65  E-value: 2.24e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148596917 257 NQRVASLLIDAGANVNVKDRNGKTPLMVAVL----NNHEELVQLLLDKGADASVKNEFGKGVLEM 317
Cdd:PHA02859  65 NVEILKFLIENGADVNFKTRDNNLSALHHYLsfnkNVEPEILKILIDSGSSITEEDEDGKNLLHM 129
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 144-215 2.33e-03

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: 39.78  E-value: 2.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917 144 GFTALMVAAQKGYTRLVKILVSNGTDVNLK-NGS-------------GKDSLMLACYAGHLDVVKYLRRHG---ASWQAR 206
Cdd:cd22193   76 GQTALHIAIERRQGDIVALLVENGADVHAHaKGRffqpkyqgegfyfGELPLSLAACTNQPDIVQYLLENEhqpADIEAQ 155


                 ....*....
gi 148596917 207 DLGGCTALH 215
Cdd:cd22193  156 DSRGNTVLH 164
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 177-202 2.66e-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: 2.66e-03
                           10        20
                   ....*....|....*....|....*.
gi 148596917   177 GKDSLMLACYAGHLDVVKYLRRHGAS 202
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGAD 27
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 144-215 2.76e-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: 39.40  E-value: 2.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917 144 GFTALMVAAQKGYTRLVKILVSNGTDVN-------LKNGSGKDS-------LMLACYAGHLDVVKYLRRH---GASWQAR 206
Cdd:cd22196   94 GQTALHIAIERRNMHLVELLVQNGADVHarasgefFKKKKGGPGfyfgelpLSLAACTNQLDIVKFLLENphsPADISAR 173


                 ....*....
gi 148596917 207 DLGGCTALH 215
Cdd:cd22196  174 DSMGNTVLH 182
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 253-315 2.88e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 39.47  E-value: 2.88e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148596917 253 AVSGNQRVASLLIDAGANVNVKDRNGKTPLMVAVLNNHEELVQLLLDKGADASVKNEFGKGVL 315
Cdd:PLN03192 533 ASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTAL 595
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 278-332 3.02e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 39.29  E-value: 3.02e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148596917  278 GKTPLMVAVLNNHEELVQLLLDKGADASVK---NEF--GKGV---------LEMARVFDRQSVVSLLEE 332
Cdd:TIGR00870 128 GITALHLAAHRQNYEIVKLLLERGASVPARacgDFFvkSQGVdsfyhgespLNAAACLGSPSIVALLSE 196
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 181-207 5.41e-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. 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: 34.19  E-value: 5.41e-03
                          10        20
                  ....*....|....*....|....*...
gi 148596917  181 LMLACY-AGHLDVVKYLRRHGASWQARD 207
Cdd:pfam00023   6 LHLAAGrRGNLEIVKLLLSKGADVNARD 33
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 219-300 8.41e-03

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 37.97  E-value: 8.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917 219 DGGHCSVIEWMIKDGCEVdvvdtgSGWTPLmRVSAVSGNQRVASL-----LIDAGANVNVKDRNGKTPLMVAVLNN---- 289
Cdd:PHA02716 478 DVYHCAIIERYNNAVCET------SGMTPL-HVSIISHTNANIVMdsfvyLLSIQYNINIPTKNGVTPLMLTMRNNrlsg 550

                         90
                 ....*....|..
gi 148596917 290 -HEELVQLLLDK 300
Cdd:PHA02716 551 hQWYIVKNILDK 562
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 152-316 9.88e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 37.80  E-value: 9.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917 152 AQKGYTRLVKILVSNGTDVNLKNGSGKDSLMLACYAGHLDVVKYLRrhgaswqardlggctalhwaadgghcsvieWMIK 231
Cdd:PHA02989  83 TSNKIKKIVKLLLKFGADINLKTFNGVSPIVCFIYNSNINNCDMLR------------------------------FLLS 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596917 232 DGCEVDVVDTGSGWTPL-MRVSAVSGNQRVASLLIDAGANV-NVKDRNGKTPLMVAVLNNHE----ELVQLLLDKGADAS 305
Cdd:PHA02989 133 KGINVNDVKNSRGYNLLhMYLESFSVKKDVIKILLSFGVNLfEKTSLYGLTPMNIYLRNDIDvisiKVIKYLIKKGVNIE 212

                        170
                 ....*....|.
gi 148596917 306 VKNEFGKGVLE 316
Cdd:PHA02989 213 TNNNGSESVLE 223
 
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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