NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1391723754|ref|NP_001350478|]
View 

fibronectin type 3 and ankyrin repeat domains protein 1 isoform 3 [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
108-335 3.83e-55

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 181.69  E-value: 3.83e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 108 LHRAVSVNDEDLLVRILQGGRVKVDVPNKFGFTALMVAAQKGYTRLVKILVSNGTDVNLKNGSGKDSLMLACYAGHLDVV 187
Cdd:COG0666    57 LLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIV 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 188 KYLRRHGASWQARDLGGCTALHWAADGGHCSVIEWMIKDGCEVDVVDtGSGWTPLMrVSAVSGNQRVASLLIDAGANVNV 267
Cdd:COG0666   137 KLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD-NDGETPLH-LAAENGHLEIVKLLLEAGADVNA 214

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1391723754 268 KDRNGKTPLMVAVLNNHEELVQLLLDKGADASVKNEFGKGVLEMARVFDRQSVVSLLEERKKKQRPKK 335
Cdd:COG0666   215 KDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 3-87 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 1391723754    3 PSKPHPPVVGKVTHHSIELYWdleKKAKRQGPQEQWFRFSIEEEDPKMHTYGIIYTGYATKHVVEGLEPRTLYRFRLKVT 82
Cdd:smart00060   1 PSPPSNLRVTDVTSTSVTLSW---EPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77


                   ....*
gi 1391723754   83 SPSGE 87
Cdd:smart00060  78 NGAGE 82
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
108-335 3.83e-55

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 181.69  E-value: 3.83e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 108 LHRAVSVNDEDLLVRILQGGRVKVDVPNKFGFTALMVAAQKGYTRLVKILVSNGTDVNLKNGSGKDSLMLACYAGHLDVV 187
Cdd:COG0666    57 LLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIV 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 188 KYLRRHGASWQARDLGGCTALHWAADGGHCSVIEWMIKDGCEVDVVDtGSGWTPLMrVSAVSGNQRVASLLIDAGANVNV 267
Cdd:COG0666   137 KLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD-NDGETPLH-LAAENGHLEIVKLLLEAGADVNA 214

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1391723754 268 KDRNGKTPLMVAVLNNHEELVQLLLDKGADASVKNEFGKGVLEMARVFDRQSVVSLLEERKKKQRPKK 335
Cdd:COG0666   215 KDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
Ank_2 pfam12796
Ankyrin repeats (3 copies);
142-234 1.81e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.49  E-value: 1.81e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 142 LMVAAQKGYTRLVKILVSNGTDVNLKNGSGKDSLMLACYAGHLDVVKYLRRHGAswQARDLGGCTALHWAADGGHCSVIE 221
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1391723754 222 WMIKDGCEVDVVD 234
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 108-304 6.28e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 89.72  E-value: 6.28e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 108 LHRAVSVNDEDLLVRILQGGrVKVDVPNKFGFTALMVAAQKGYT-----RLVKILVSNGTDVNlkNGSGKDSLMLACYA- 181
Cdd:PHA03100   39 LYLAKEARNIDVVKILLDNG-ADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVN--APDNNGITPLLYAIs 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 182 ---GHLDVVKYLRRHGASWQARDLGGCTALHWAADGGH------------------CSVIEWMIKDGCEVDVVDTgSGWT 240
Cdd:PHA03100  116 kksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidlkilkllidkgvdinaKNRVNYLLSYGVPINIKDV-YGFT 194

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1391723754 241 PLMrvSAV-SGNQRVASLLIDAGANVNVKDRNGKTPLMVAVLNNHEELVQLLLDKGADASVKNEF 304
Cdd:PHA03100  195 PLH--YAVyNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 3-87 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 1391723754    3 PSKPHPPVVGKVTHHSIELYWdleKKAKRQGPQEQWFRFSIEEEDPKMHTYGIIYTGYATKHVVEGLEPRTLYRFRLKVT 82
Cdd:smart00060   1 PSPPSNLRVTDVTSTSVTLSW---EPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77


                   ....*
gi 1391723754   83 SPSGE 87
Cdd:smart00060  78 NGAGE 82
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 271-297 1.04e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 44.50  E-value: 1.04e-06
                           10        20
                   ....*....|....*....|....*..
gi 1391723754  271 NGKTPLMVAVLNNHEELVQLLLDKGAD 297
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 140-293 1.96e-06

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 49.24  E-value: 1.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 140 TALMVAAQKGYTRLVK-ILVSNGTDVNLKNGSGKDSLMLACYAGHLDVVKYLRRhgaswQARDL----------GGCTAL 208
Cdd:cd22192    19 SPLLLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME-----AAPELvnepmtsdlyQGETAL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 209 HWAADGGHCSVIEWMIKDGceVDVVD---TGSGWTP-----------LMRVSAVSGNQRVASLLIDAGANVNVKDRNGKT 274
Cdd:cd22192    94 HIAVVNQNLNLVRELIARG--ADVVSpraTGTFFRPgpknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNT 171

                         170
                  ....*....|....*....
gi 1391723754 275 PLMVAVLNNHEELVQLLLD 293
Cdd:cd22192   172 VLHILVLQPNKTFACQMYD 190
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 3-98 3.69e-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: 3.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754   3 PSKPHPPVVGKVTHHSIELYWDlekkaKRQGPQEQWFRFSIEEEDPKMHTYGIIYTGY--ATKHVVEGLEPRTLYRFRLK 80
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWT-----PPEDDGGPITGYVVEYREKGSGDWKEVEVTPgsETSYTLTGLKPGTEYEFRVR 75

                          90
                  ....*....|....*...
gi 1391723754  81 VTSPSGECEYSPLVSVST 98
Cdd:cd00063    76 AVNGGGESPPSESVTVTT 93
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 137-209 1.72e-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: 1.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 137 FGFTALMVAAQKGYTRLVKILVSNGTDVNLK-------NGSGKDSLM-----LACYA--GHLDVVKYLRRHGASWQARDL 202
Cdd:TIGR00870 127 PGITALHLAAHRQNYEIVKLLLERGASVPARacgdffvKSQGVDSFYhgespLNAAAclGSPSIVALLSEDPADILTADS 206


                  ....*..
gi 1391723754 203 GGCTALH 209
Cdd:TIGR00870 207 LGNTLLH 213
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
108-335 3.83e-55

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 181.69  E-value: 3.83e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 108 LHRAVSVNDEDLLVRILQGGRVKVDVPNKFGFTALMVAAQKGYTRLVKILVSNGTDVNLKNGSGKDSLMLACYAGHLDVV 187
Cdd:COG0666    57 LLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIV 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 188 KYLRRHGASWQARDLGGCTALHWAADGGHCSVIEWMIKDGCEVDVVDtGSGWTPLMrVSAVSGNQRVASLLIDAGANVNV 267
Cdd:COG0666   137 KLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD-NDGETPLH-LAAENGHLEIVKLLLEAGADVNA 214

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1391723754 268 KDRNGKTPLMVAVLNNHEELVQLLLDKGADASVKNEFGKGVLEMARVFDRQSVVSLLEERKKKQRPKK 335
Cdd:COG0666   215 KDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
107-334 1.34e-52

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 175.14  E-value: 1.34e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 107 HLHRAVSVNDEDLLVRILQGGRVKVDVPNKFGFTALMVAAQKGYTRLVKILVSNGTDVNLKNGSGKDSLMLACYAGHLDV 186
Cdd:COG0666    23 LLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEI 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 187 VKYLRRHGASWQARDLGGCTALHWAADGGHCSVIEWMIKDGCEVDVVDtGSGWTPLMrVSAVSGNQRVASLLIDAGANVN 266
Cdd:COG0666   103 VKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQD-NDGNTPLH-LAAANGNLEIVKLLLEAGADVN 180

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1391723754 267 VKDRNGKTPLMVAVLNNHEELVQLLLDKGADASVKNEFGKGVLEMARVFDRQSVVSLLEERKKKQRPK 334
Cdd:COG0666   181 ARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAK 248
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
118-328 2.60e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 143.17  E-value: 2.60e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 118 DLLVRILQGGRVKVDVPNKFGFTALMVAAQKGYTRLVKILVSNGTDVNLKNGSGKDSLMLACYAGHLDVVKYLRRHGASW 197
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 198 QARDLGGCTALHWAADGGHCSVIEWMIKDGCEVDVVDTgSGWTPLMrVSAVSGNQRVASLLIDAGANVNVKDRNGKTPLM 277
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDK-DGETPLH-LAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLH 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1391723754 278 VAVLNNHEELVQLLLDKGADASVKNEFGKGVLEMARVFDRQSVVSLLEERK 328
Cdd:COG0666   159 LAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAG 209
Ank_2 pfam12796
Ankyrin repeats (3 copies);
142-234 1.81e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.49  E-value: 1.81e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 142 LMVAAQKGYTRLVKILVSNGTDVNLKNGSGKDSLMLACYAGHLDVVKYLRRHGAswQARDLGGCTALHWAADGGHCSVIE 221
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1391723754 222 WMIKDGCEVDVVD 234
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
208-302 2.24e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.40  E-value: 2.24e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 208 LHWAADGGHCSVIEWMIKDGCEVDVVDTgSGWTPLMrVSAVSGNQRVASLLIDaGANVNVKDrNGKTPLMVAVLNNHEEL 287
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDK-NGRTALH-LAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEI 76

                          90
                  ....*....|....*
gi 1391723754 288 VQLLLDKGADASVKN 302
Cdd:pfam12796  77 VKLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 108-304 6.28e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 89.72  E-value: 6.28e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 108 LHRAVSVNDEDLLVRILQGGrVKVDVPNKFGFTALMVAAQKGYT-----RLVKILVSNGTDVNlkNGSGKDSLMLACYA- 181
Cdd:PHA03100   39 LYLAKEARNIDVVKILLDNG-ADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVN--APDNNGITPLLYAIs 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 182 ---GHLDVVKYLRRHGASWQARDLGGCTALHWAADGGH------------------CSVIEWMIKDGCEVDVVDTgSGWT 240
Cdd:PHA03100  116 kksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidlkilkllidkgvdinaKNRVNYLLSYGVPINIKDV-YGFT 194

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1391723754 241 PLMrvSAV-SGNQRVASLLIDAGANVNVKDRNGKTPLMVAVLNNHEELVQLLLDKGADASVKNEF 304
Cdd:PHA03100  195 PLH--YAVyNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
Ank_2 pfam12796
Ankyrin repeats (3 copies);
108-201 3.38e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.93  E-value: 3.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 108 LHRAVSVNDEDLLVRILQGGrVKVDVPNKFGFTALMVAAQKGYTRLVKILVSNGtDVNLKNgSGKDSLMLACYAGHLDVV 187
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKD-NGRTALHYAARSGHLEIV 77

                          90
                  ....*....|....
gi 1391723754 188 KYLRRHGASWQARD 201
Cdd:pfam12796  78 KLLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 116-321 6.41e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 84.24  E-value: 6.41e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 116 DEDLLVRILQGGrVKVDVPNKFGFTALMVAAQKGYTRLVKILVSNGTDVNLKNGSGKDSLMLACYAGHLDVVKYLRRHGA 195
Cdd:PHA02874  103 EKDMIKTILDCG-IDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGA 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 196 SWQARDLGGCTALHWAADGGHCSVIEWMIKDGCEVdVVDTGSGWTPLMrvSAVSGNQRVASLLIDaGANVNVKDRNGKTP 275
Cdd:PHA02874  182 YANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHI-MNKCKNGFTPLH--NAIIHNRSAIELLIN-NASINDQDIDGSTP 257

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1391723754 276 LMVAV-LNNHEELVQLLLDKGADASVKNEFGKGVLEMA-RVFDRQSVV 321
Cdd:PHA02874  258 LHHAInPPCDIDIIDILLYHKADISIKDNKGENPIDTAfKYINKDPVI 305
PHA03095 PHA03095
ankyrin-like protein; Provisional
 118-300 8.66e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 77.76  E-value: 8.66e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 118 DLLVRilQGGRVkvDVPNKFGFTALMVAAQKGYTR--LVKILVSNGTDVNLKNGSGKDSLmlACY--------------- 180
Cdd:PHA03095  101 KLLIK--AGADV--NAKDKVGRTPLHVYLSGFNINpkVIRLLLRKGADVNALDLYGMTPL--AVLlksrnanvellrlli 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 181 -AG----------------HLD-------VVKYLRRHGASWQARDLGGCTALHWAADGGHC--SVIEWMIKDGCEVDVVD 234
Cdd:PHA03095  175 dAGadvyavddrfrsllhhHLQsfkprarIVRELIRAGCDPAATDMLGNTPLHSMATGSSCkrSLVLPLLIAGISINARN 254

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1391723754 235 TgSGWTPLMrVSAVSGNQRVASLLIDAGANVNVKDRNGKTPLMVAVLNNHEELVQLLLDKGADASV 300
Cdd:PHA03095  255 R-YGQTPLH-YAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAET 318
PHA03095 PHA03095
ankyrin-like protein; Provisional
 115-327 2.03e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 73.91  E-value: 2.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 115 NDEDLLVRILQGGRVKVDVpnkfgftalmvaaqkgytrlVKILVSNGTDVNLKNGSGKDSL-MLACYAGH--LDVVKYLR 191
Cdd:PHA03095   11 MEAALYDYLLNASNVTVEE--------------------VRRLLAAGADVNFRGEYGKTPLhLYLHYSSEkvKDIVRLLL 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 192 RHGASWQARDLGGCTALH-WAADGGHCSVIEWMIKDGCEVDVVDtGSGWTPL-MRVSAVSGNQRVASLLIDAGANVNVKD 269
Cdd:PHA03095   71 EAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKD-KVGRTPLhVYLSGFNINPKVIRLLLRKGADVNALD 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1391723754 270 RNGKTPLMVAVLNNH--EELVQLLLDKGADASVKNEFGKGVLE-MARVF-DRQSVVSLLEER 327
Cdd:PHA03095  150 LYGMTPLAVLLKSRNanVELLRLLIDAGADVYAVDDRFRSLLHhHLQSFkPRARIVRELIRA 211
PHA03095 PHA03095
ankyrin-like protein; Provisional
 131-318 5.40e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 72.36  E-value: 5.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 131 VDVPNKFGFTALMVAAQKGYT-RLVKILVSNGTDVNLKNGSGKDSLMlACYAG---HLDVVKYLRRHGASWQARDLGGCT 206
Cdd:PHA03095   76 VNAPERCGFTPLHLYLYNATTlDVIKLLIKAGADVNAKDKVGRTPLH-VYLSGfniNPKVIRLLLRKGADVNALDLYGMT 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 207 ALHWAADGGHCSV--IEWMIKDGCEVDVVDTgSGWTPL--MRVSAVSgNQRVASLLIDAGANVNVKDRNGKTPL--MVAV 280
Cdd:PHA03095  155 PLAVLLKSRNANVelLRLLIDAGADVYAVDD-RFRSLLhhHLQSFKP-RARIVRELIRAGCDPAATDMLGNTPLhsMATG 232

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1391723754 281 LNNHEELVQLLLDKGADASVKNEFGKGVLEMARVFDRQ 318
Cdd:PHA03095  233 SSCKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNP 270
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 108-302 1.36e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 71.63  E-value: 1.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 108 LHRAVSVNDEDLLV-RILQGGrVKVDVPNKFGFTALMVAAQKGY-TRLVKILVSNGTDVNLKNGSGKDSLMLACYAG-HL 184
Cdd:PHA02876  277 LHHASQAPSLSRLVpKLLERG-ADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDrNK 355

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 185 DVVKYLRRHGASWQARDLGGCTALHWAADGGHCSVIEWMIKDGCEVDVVDTGSGwTPLMrvSAVSGNQRVASL--LIDAG 262
Cdd:PHA02876  356 DIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIG-TALH--FALCGTNPYMSVktLIDRG 432

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1391723754 263 ANVNVKDRNGKTPLMVAVLNNHE-ELVQLLLDKGADASVKN 302
Cdd:PHA02876  433 ANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAIN 473
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 145-300 1.84e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 70.79  E-value: 1.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 145 AAQKGYTRLVKILVSNGT---DVNLKNGSgkDSLMLACYAGHLDVVKYLRRHGASWQARDLGGCTALHWAADGGHCSVIE 221
Cdd:PHA02875   75 AVEEGDVKAVEELLDLGKfadDVFYKDGM--TPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIE 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 222 WMIKDGCEVDVVDtGSGWTPLMrVSAVSGNQRVASLLIDAGANVNVKDRNGKTPLM-VAVLNNHEELVQLLLDKGADASV 300
Cdd:PHA02875  153 LLIDHKACLDIED-CCGCTPLI-IAMAKGDIAICKMLLDSGANIDYFGKNGCVAALcYAIENNKIDIVRLFIKRGADCNI 230
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 116-325 7.00e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 69.32  E-value: 7.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 116 DEDLLVRILQGGRVKVDVPNKFGFTALMVAAQKGYTRLVKILVSNGTDVNLKNGSGKDSLMLACYAGHLDVVKYLRRHGA 195
Cdd:PHA02876  156 DELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRS 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 196 SWQARDLGGCTALhwAADGGHCSVIewMIKDGCEVDVVDTGSGwTPLMRVSAVSGNQRVASLLIDAGANVNVKDRNGKTP 275
Cdd:PHA02876  236 NINKNDLSLLKAI--RNEDLETSLL--LYDAGFSVNSIDDCKN-TPLHHASQAPSLSRLVPKLLERGADVNAKNIKGETP 310

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1391723754 276 LMVAVLNNHE-ELVQLLLDKGADASVKNEFGKGVLEMARVFDR--QSVVSLLE 325
Cdd:PHA02876  311 LYLMAKNGYDtENIRTLIMLGADVNAADRLYITPLHQASTLDRnkDIVITLLE 363
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 117-281 7.18e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 66.06  E-value: 7.18e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 117 EDLLVRIL--QGGRVKVDVPNKfGFTALMVAAQKGYTRLVKILVSNGTDVNLKNGSGKDSLMLACYAGHLDVVKYLRRHG 194
Cdd:PHA02878  146 EAEITKLLlsYGADINMKDRHK-GNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENG 224

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 195 ASWQARDLGGCTALHWAAdgGHC---SVIEWMIKDGCEVDVVDTGSGWTPLMrvSAVSgNQRVASLLIDAGANVNVKDRN 271
Cdd:PHA02878  225 ASTDARDKCGNTPLHISV--GYCkdyDILKLLLEHGVDVNAKSYILGLTALH--SSIK-SERKLKLLLEYGADINSLNSY 299

                         170
                  ....*....|
gi 1391723754 272 GKTPLMVAVL 281
Cdd:PHA02878  300 KLTPLSSAVK 309
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 140-324 1.19e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 65.37  E-value: 1.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 140 TALMVAAQKGYTRLVKILVSNGTDVNLKNGSGKDSLMLACYAGHLDVVKYLRRHGASW---------------------- 197
Cdd:PHA02874   37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTsilpipciekdmiktildcgid 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 198 -QARDLGGCTALHWAADGGHCSVIEWMIKDGCEVDVVDTgSGWTPLmRVSAVSGNQRVASLLIDAGANVNVKDRNGKTPL 276
Cdd:PHA02874  117 vNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDD-NGCYPI-HIAIKHNFFDIIKLLLEKGAYANVKDNNGESPL 194

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1391723754 277 MVAVLNNHEELVQLLLDKGADASVKNEFGKGVLEMARVFDRqSVVSLL 324
Cdd:PHA02874  195 HNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELL 241
Ank_2 pfam12796
Ankyrin repeats (3 copies);
242-324 2.97e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.97  E-value: 2.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 242 LMrVSAVSGNQRVASLLIDAGANVNVKDRNGKTPLMVAVLNNHEELVQLLLDKgADASVKNEfGKGVLEMARVFDRQSVV 321
Cdd:pfam12796   1 LH-LAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIV 77


                  ...
gi 1391723754 322 SLL 324
Cdd:pfam12796  78 KLL 80
Ank_4 pfam13637
Ankyrin repeats (many copies);
175-224 3.29e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 57.67  E-value: 3.29e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1391723754 175 LMLACYAGHLDVVKYLRRHGASWQARDLGGCTALHWAADGGHCSVIEWMI 224
Cdd:pfam13637   5 LHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 142-304 4.00e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 64.12  E-value: 4.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 142 LMVAAQKGYTRLVKILVSNGTDVNLKNGSGKDSLMLACYAGHLDVVKYLRRHGASWQARDLGGCTALHWAADGGHCSvIE 221
Cdd:PLN03192  529 LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHK-IF 607

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 222 WMIKDGCEVDVVDTGSGwtpLMRVSAVSGNQRVASLLIDAGANVNVKDRNGKTPLMVAVLNNHEELVQLLLDKGAD---A 298
Cdd:PLN03192  608 RILYHFASISDPHAAGD---LLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADvdkA 684


                  ....*.
gi 1391723754 299 SVKNEF 304
Cdd:PLN03192  685 NTDDDF 690
Ank_5 pfam13857
Ankyrin repeats (many copies);
258-312 4.86e-10

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 54.66  E-value: 4.86e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1391723754 258 LIDAG-ANVNVKDRNGKTPLMVAVLNNHEELVQLLLDKGADASVKNEFGKGVLEMA 312
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 247-324 9.80e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 59.91  E-value: 9.80e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1391723754 247 AVSGNQRVASLLIDAGANVNVKDRNGKTPLMVAVLNNHEELVQLLLDKGADASVKNEFGKGVLEMARVFDRQSVVSLL 324
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
Ank_4 pfam13637
Ankyrin repeats (many copies);
238-292 4.25e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.89  E-value: 4.25e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1391723754 238 GWTPLMRVsAVSGNQRVASLLIDAGANVNVKDRNGKTPLMVAVLNNHEELVQLLL 292
Cdd:pfam13637   1 ELTALHAA-AASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
140-190 4.82e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.89  E-value: 4.82e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1391723754 140 TALMVAAQKGYTRLVKILVSNGTDVNLKNGSGKDSLMLACYAGHLDVVKYL 190
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 219-327 1.44e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 56.04  E-value: 1.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 219 VIEWMIKDGCEVDVVDTGSGWTPLmRVSAVSGNQRVASLLIDAGANVNVKDRNGKTPLMVAVLNNHEELVQLLLDKGADA 298
Cdd:PHA02878  149 ITKLLLSYGADINMKDRHKGNTAL-HYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAST 227

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1391723754 299 SVKNEFGKGVLEMA--RVFDrQSVVSLLEER 327
Cdd:PHA02878  228 DARDKCGNTPLHISvgYCKD-YDILKLLLEH 257
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 101-242 1.49e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 56.03  E-value: 1.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 101 EPISSEHLHRAVSVNDEDLLVRILQGGRvKVDVPNKFGFTALMVAAQKGYTRLVKILVSNGTDVNLKNGSGKDSLMLACY 180
Cdd:PLN03192  522 DPNMASNLLTVASTGNAALLEELLKAKL-DPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAIS 600

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 181 AGH-------------------------------LDVVKYLRRHGASWQARDLGGCTALHWAADGGHCSVIEWMIKDGCE 229
Cdd:PLN03192  601 AKHhkifrilyhfasisdphaagdllctaakrndLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGAD 680

                         170
                  ....*....|...
gi 1391723754 230 VDVVDTGSGWTPL 242
Cdd:PLN03192  681 VDKANTDDDFSPT 693
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 111-327 1.86e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 55.38  E-value: 1.86e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 111 AVSVNDEDLLVRILQGG-RVKVDVPNkfGFTALMVAAQKGYTRLVKILVSNGTDVNLKNGSGKDSLMLACYAGHLDVVKY 189
Cdd:PHA02875    9 AILFGELDIARRLLDIGiNPNFEIYD--GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEE 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 190 LRRHGASwqARDL---GGCTALHWAADGGHCSVIEWMIKDGCEVDVVDTGSgWTPLmRVSAVSGNQRVASLLIDAGANVN 266
Cdd:PHA02875   87 LLDLGKF--ADDVfykDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDK-FSPL-HLAVMMGDIKGIELLIDHKACLD 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1391723754 267 VKDRNGKTPLMVAVLNNHEELVQLLLDKGADAsvkNEFGK----GVLEMARVFDRQSVVSLLEER 327
Cdd:PHA02875  163 IEDCCGCTPLIIAMAKGDIAICKMLLDSGANI---DYFGKngcvAALCYAIENNKIDIVRLFIKR 224
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
108-208 1.86e-08

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 54.96  E-value: 1.86e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 108 LHRAVSVNDEDLlVRILQGGRVKVDVPNKFGFTALMVAAQKGYTRLVKILVSNGTDVNLKNGSGKDSLMLACYAGHLDVV 187
Cdd:COG0666   190 LHLAAENGHLEI-VKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIV 268

                          90       100
                  ....*....|....*....|.
gi 1391723754 188 KYLRRHGASWQARDLGGCTAL 208
Cdd:COG0666   269 KLLLLALLLLAAALLDLLTLL 289
Ank_5 pfam13857
Ankyrin repeats (many copies);
157-211 7.54e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.50  E-value: 7.54e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1391723754 157 LVSNGT-DVNLKNGSGKDSLMLACYAGHLDVVKYLRRHGASWQARDLGGCTALHWA 211
Cdd:pfam13857   1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 3-87 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 1391723754    3 PSKPHPPVVGKVTHHSIELYWdleKKAKRQGPQEQWFRFSIEEEDPKMHTYGIIYTGYATKHVVEGLEPRTLYRFRLKVT 82
Cdd:smart00060   1 PSPPSNLRVTDVTSTSVTLSW---EPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77


                   ....*
gi 1391723754   83 SPSGE 87
Cdd:smart00060  78 NGAGE 82
Ank_5 pfam13857
Ankyrin repeats (many copies);
123-178 8.69e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.42  E-value: 8.69e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1391723754 123 ILQGGRVKVDVPNKFGFTALMVAAQKGYTRLVKILVSNGTDVNLKNGSGKDSLMLA 178
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 271-297 1.04e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 44.50  E-value: 1.04e-06
                           10        20
                   ....*....|....*....|....*..
gi 1391723754  271 NGKTPLMVAVLNNHEELVQLLLDKGAD 297
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 140-293 1.96e-06

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 49.24  E-value: 1.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 140 TALMVAAQKGYTRLVK-ILVSNGTDVNLKNGSGKDSLMLACYAGHLDVVKYLRRhgaswQARDL----------GGCTAL 208
Cdd:cd22192    19 SPLLLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME-----AAPELvnepmtsdlyQGETAL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 209 HWAADGGHCSVIEWMIKDGceVDVVD---TGSGWTP-----------LMRVSAVSGNQRVASLLIDAGANVNVKDRNGKT 274
Cdd:cd22192    94 HIAVVNQNLNLVRELIARG--ADVVSpraTGTFFRPgpknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNT 171

                         170
                  ....*....|....*....
gi 1391723754 275 PLMVAVLNNHEELVQLLLD 293
Cdd:cd22192   172 VLHILVLQPNKTFACQMYD 190
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 223-292 2.14e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.51  E-value: 2.14e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 223 MIKDGCEVDVVDTgSGWTPLmRVSAVSGNQRVASLLIDAGANVNVKDRNGKTPLMVAVLNNHEELVQLLL 292
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 ...
 3-98 3.69e-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: 3.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754   3 PSKPHPPVVGKVTHHSIELYWDlekkaKRQGPQEQWFRFSIEEEDPKMHTYGIIYTGY--ATKHVVEGLEPRTLYRFRLK 80
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWT-----PPEDDGGPITGYVVEYREKGSGDWKEVEVTPgsETSYTLTGLKPGTEYEFRVR 75

                          90
                  ....*....|....*...
gi 1391723754  81 VTSPSGECEYSPLVSVST 98
Cdd:cd00063    76 AVNGGGESPPSESVTVTT 93
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 271-303 4.82e-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: 42.66  E-value: 4.82e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1391723754 271 NGKTPLMVAVL-NNHEELVQLLLDKGADASVKNE 303
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
189-242 9.26e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 9.26e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1391723754 189 YLRRHGASWQARDLGGCTALHWAADGGHCSVIEWMIKDGCEVDVVDtGSGWTPL 242
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKD-EEGLTAL 53
PHA02798 PHA02798
ankyrin-like protein; Provisional
 153-312 1.01e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 47.14  E-value: 1.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 153 LVKILVSNGTDVNLKNGSGKDSL--MLA-CYAGHLDVVKYLRRHGASWQARDLGGCTALHWAADGGH---CSVIEWMIKD 226
Cdd:PHA02798   91 IVKILIENGADINKKNSDGETPLycLLSnGYINNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEK 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 227 GCEVDVVDTGSGWTPL---------------------------------------MRVSAVSGNQRVASLLID---AGAN 264
Cdd:PHA02798  171 GVDINTHNNKEKYDTLhcyfkynidridadilklfvdngfiinkenkshkkkfmeYLNSLLYDNKRFKKNILDfifSYID 250

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1391723754 265 VNVKDRNGKTPLMVAVLNNHEELVQLLLDKGADASVKNEFGKGVLEMA 312
Cdd:PHA02798  251 INQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTA 298
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 215-310 1.27e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 46.50  E-value: 1.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 215 GHCSVIEWMIKDGCEVDVVDTGSGWTPLmrVSAV-SGNQRVASLLIDAGANVNVKDRNGKTPLMVAVLNNHEELVQLLLD 293
Cdd:PHA02874   12 GDIEAIEKIIKNKGNCINISVDETTTPL--IDAIrSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLID 89

                          90       100
                  ....*....|....*....|...
gi 1391723754 294 KGADASV------KNEFGKGVLE 310
Cdd:PHA02874   90 NGVDTSIlpipciEKDMIKTILD 112
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 238-270 1.48e-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: 1.48e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1391723754 238 GWTPLMRVSAVSGNQRVASLLIDAGANVNVKDR 270
Cdd:pfam00023   2 GNTPLHLAAGRRGNLEIVKLLLSKGADVNARDK 34
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 271-300 1.60e-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: 1.60e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 1391723754 271 NGKTPLMVAVLNNHEELVQLLLDKGADASV 300
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02798 PHA02798
ankyrin-like protein; Provisional
 184-305 2.15e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 45.98  E-value: 2.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 184 LDVVKYLRRHGASWQARD----LGGCTALHWAADGGH-CSVIEWMIKDGCEVDVVDTgSGWTPL--MRVSAVSGNQRVAS 256
Cdd:PHA02798   51 TDIVKLFINLGANVNGLDneysTPLCTILSNIKDYKHmLDIVKILIENGADINKKNS-DGETPLycLLSNGYINNLEILL 129

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1391723754 257 LLIDAGANVNVKDRNGKTPLMVAVLNNHE---ELVQLLLDKGADASV-KNEFG 305
Cdd:PHA02798  130 FMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDINThNNKEK 182
PHA02798 PHA02798
ankyrin-like protein; Provisional
 90-267 2.33e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 45.98  E-value: 2.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754  90 YSPLVSVSTTREPISSEHLHraVSVNDEDLLVRILQGGRVKVDVpnkfgftalmvaaqkgytrlVKILVSNGTDVNlkng 169
Cdd:PHA02798   12 FSDNVKLSTVKLLIKSCNPN--EIVNEYSIFQKYLQRDSPSTDI--------------------VKLFINLGANVN---- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 170 sGKDSLM----------LACYAGHLDVVKYLRRHGASWQARDLGGCTALHWAADGGHCSVIE---WMIKDGCEVDVVDtG 236
Cdd:PHA02798   66 -GLDNEYstplctilsnIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEillFMIENGADTTLLD-K 143

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1391723754 237 SGWTPLmRVSAVSGNQ---RVASLLIDAGANVNV 267
Cdd:PHA02798  144 DGFTML-QVYLQSNHHidiEIIKLLLEKGVDINT 176
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 138-168 3.94e-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: 39.97  E-value: 3.94e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1391723754 138 GFTALMVAA-QKGYTRLVKILVSNGTDVNLKN 168
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 138-209 4.50e-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: 4.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 138 GFTALMVAAQKGYTRLVKILVSNGTDVNLK-NGS------------GKDSLMLACYAGHLDVVKYLRRHG---ASWQARD 201
Cdd:cd21882    73 GQTALHIAIENRNLNLVRLLVENGADVSARaTGRffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGaqpAALEAQD 152


                  ....*...
gi 1391723754 202 LGGCTALH 209
Cdd:cd21882   153 SLGNTVLH 160
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 138-209 7.66e-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: 7.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 138 GFTALMVAAQKGYTRLVKILVSNGTDVNL---------KNGS----GKDSLMLACYAGHLDVVKYL---RRHGASWQARD 201
Cdd:cd22197    94 GHSALHIAIEKRSLQCVKLLVENGADVHAracgrffqkKQGTcfyfGELPLSLAACTKQWDVVNYLlenPHQPASLQAQD 173


                  ....*...
gi 1391723754 202 LGGCTALH 209
Cdd:cd22197   174 SLGNTVLH 181
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 108-251 1.07e-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: 1.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 108 LHRAVSVNDEDLLVRILQGGRVKVDVPNK----FGFTALMVAAQKGYTRLVKILVSNGTDVNLKNGSG------KDSLML 177
Cdd:cd22192    55 LHVAALYDNLEAAVVLMEAAPELVNEPMTsdlyQGETALHIAVVNQNLNLVRELIARGADVVSPRATGtffrpgPKNLIY 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 178 ---------ACyAGHLDVVKYLRRHGASWQARDLGGCTALH----WAADGGHCSVIEWMI-----KDGCEVDVVDTGSGW 239
Cdd:cd22192   135 ygehplsfaAC-VGNEEIVRLLIEHGADIRAQDSLGNTVLHilvlQPNKTFACQMYDLILsydkeDDLQPLDLVPNNQGL 213

                         170
                  ....*....|..
gi 1391723754 240 TPlMRVSAVSGN 251
Cdd:cd22192   214 TP-FKLAAKEGN 224
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 253-309 1.58e-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: 1.58e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1391723754 253 RVASLLIDAGANVNV---------KDRN-----GKTPLMVAVLNNHEELVQLLLDKGAD-ASVKNEFGKGVL 309
Cdd:cd22194   155 DIVKLLIAKGADVNAhakgvffnpKYKHegfyfGETPLALAACTNQPEIVQLLMEKESTdITSQDSRGNTVL 226
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 137-209 1.72e-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: 1.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 137 FGFTALMVAAQKGYTRLVKILVSNGTDVNLK-------NGSGKDSLM-----LACYA--GHLDVVKYLRRHGASWQARDL 202
Cdd:TIGR00870 127 PGITALHLAAHRQNYEIVKLLLERGASVPARacgdffvKSQGVDSFYhgespLNAAAclGSPSIVALLSEDPADILTADS 206


                  ....*..
gi 1391723754 203 GGCTALH 209
Cdd:TIGR00870 207 LGNTLLH 213
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 219-309 2.34e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 41.73  E-value: 2.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 219 VIEWMIKDGCEVDVVDTGSGWTPLMRVSAVSGN--QRVASLLIDAGANVNVKDRNGKTPLMVAV--LNNHEELVQLLLDK 294
Cdd:PHA02859   68 ILKFLIENGADVNFKTRDNNLSALHHYLSFNKNvePEILKILIDSGSSITEEDEDGKNLLHMYMcnFNVRINVIKLLIDS 147

                          90
                  ....*....|....*
gi 1391723754 295 GADASVKNEFGKGVL 309
Cdd:PHA02859  148 GVSFLNKDFDNNNIL 162
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 253-337 3.10e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 42.17  E-value: 3.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 253 RVASLLIDAGANVNVKDRN-GKTPLMVAVLNNHEELVQLLLDKGADASVKNEFGKGVLEMARVFDRQSVVSLLEERKKKQ 331
Cdd:PHA02878  148 EITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAST 227


                  ....*.
gi 1391723754 332 RPKKSC 337
Cdd:PHA02878  228 DARDKC 233
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 204-232 3.23e-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: 3.23e-04
                          10        20
                  ....*....|....*....|....*....
gi 1391723754 204 GCTALHWAADGGHCSVIEWMIKDGCEVDV 232
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 138-166 3.56e-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: 37.18  E-value: 3.56e-04
                           10        20
                   ....*....|....*....|....*....
gi 1391723754  138 GFTALMVAAQKGYTRLVKILVSNGTDVNL 166
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 146-221 4.70e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.81  E-value: 4.70e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1391723754 146 AQKGYTRLVKILVSNGTDVNLKNGSGKDSLMLACYAGHLDVVKYLRRHGASWQARDLGGCTALHWAADGGHCSVIE 221
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 204-234 4.87e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.88  E-value: 4.87e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1391723754 204 GCTALHWAAD-GGHCSVIEWMIKDGCEVDVVD 234
Cdd:pfam00023   2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 206-297 4.94e-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: 4.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 206 TALHWAADGGHCSVIEWMIKdgCE-VDVVDTGS-GWTPLmRVSAVSGNQRVASLLIDAGAN-VNVKDRN----GKTPLMV 278
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLK--CPsCDLFQRGAlGETAL-HVAALYDNLEAAVVLMEAAPElVNEPMTSdlyqGETALHI 95

                          90
                  ....*....|....*....
gi 1391723754 279 AVLNNHEELVQLLLDKGAD 297
Cdd:cd22192    96 AVVNQNLNLVRELIARGAD 114
PHA02795 PHA02795
ankyrin-like protein; Provisional
 123-236 8.36e-04

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 41.13  E-value: 8.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 123 ILQGGRVKVDVPNKFGFTALMVAAQKGYTRLVKILVSNGTDVNLKNGSGKDSLMLACYAGHLDVVKYLRRHGASWQARDL 202
Cdd:PHA02795  173 IPDENDVKLDLYKIIQYTRGFLVDEPTVLEIYKLCIPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMS 252

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1391723754 203 GGCTALHWAADGG--------HCSVIEWMIKDGCEVDVVDTG 236
Cdd:PHA02795  253 NGYTCLDVAVDRGsviarretHLKILEILLREPLSIDCIKLA 294
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 185-311 8.81e-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: 8.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 185 DVVKYLRRHGASWQARDLGGCTALHWAADGGHCSVIEWMIKDGCE-VDVVDTGS---GWTPLmRVSAVSGNQRVASLLID 260
Cdd:cd22192    32 AIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPMTSDlyqGETAL-HIAVVNQNLNLVRELIA 110

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1391723754 261 AGANVnVKDRN---------------GKTPLMVAVLNNHEELVQLLLDKGADASVKNEFGKGVLEM 311
Cdd:cd22192   111 RGADV-VSPRAtgtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175
Ank_4 pfam13637
Ankyrin repeats (many copies);
274-312 1.39e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.48  E-value: 1.39e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1391723754 274 TPLMVAVLNNHEELVQLLLDKGADASVKNEFGKGVLEMA 312
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFA 41
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 204-232 1.77e-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: 1.77e-03
                           10        20
                   ....*....|....*....|....*....
gi 1391723754  204 GCTALHWAADGGHCSVIEWMIKDGCEVDV 232
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 251-311 2.18e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 38.65  E-value: 2.18e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1391723754 251 NQRVASLLIDAGANVNVKDRNGKTPLMVAVL----NNHEELVQLLLDKGADASVKNEFGKGVLEM 311
Cdd:PHA02859   65 NVEILKFLIENGADVNFKTRDNNLSALHHYLsfnkNVEPEILKILIDSGSSITEEDEDGKNLLHM 129
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 138-209 2.26e-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: 2.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 138 GFTALMVAAQKGYTRLVKILVSNGTDVNLK-NGS-------------GKDSLMLACYAGHLDVVKYLRRHG---ASWQAR 200
Cdd:cd22193    76 GQTALHIAIERRQGDIVALLVENGADVHAHaKGRffqpkyqgegfyfGELPLSLAACTNQPDIVQYLLENEhqpADIEAQ 155


                  ....*....
gi 1391723754 201 DLGGCTALH 209
Cdd:cd22193   156 DSRGNTVLH 164
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 138-209 2.68e-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: 2.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 138 GFTALMVAAQKGYTRLVKILVSNGTDVN-------LKNGSGKDS-------LMLACYAGHLDVVKYLRRH---GASWQAR 200
Cdd:cd22196    94 GQTALHIAIERRNMHLVELLVQNGADVHarasgefFKKKKGGPGfyfgelpLSLAACTNQLDIVKFLLENphsPADISAR 173


                  ....*....
gi 1391723754 201 DLGGCTALH 209
Cdd:cd22196   174 DSMGNTVLH 182
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 171-196 2.75e-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: 2.75e-03
                           10        20
                   ....*....|....*....|....*.
gi 1391723754  171 GKDSLMLACYAGHLDVVKYLRRHGAS 196
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGAD 27
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 247-309 2.80e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 39.47  E-value: 2.80e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1391723754 247 AVSGNQRVASLLIDAGANVNVKDRNGKTPLMVAVLNNHEELVQLLLDKGADASVKNEFGKGVL 309
Cdd:PLN03192  533 ASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTAL 595
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 272-326 2.93e-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: 2.93e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1391723754 272 GKTPLMVAVLNNHEELVQLLLDKGADASVK---NEF--GKGV---------LEMARVFDRQSVVSLLEE 326
Cdd:TIGR00870 128 GITALHLAAHRQNYEIVKLLLERGASVPARacgDFFvkSQGVdsfyhgespLNAAACLGSPSIVALLSE 196
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 175-201 6.10e-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: 33.80  E-value: 6.10e-03
                          10        20
                  ....*....|....*....|....*...
gi 1391723754 175 LMLACY-AGHLDVVKYLRRHGASWQARD 201
Cdd:pfam00023   6 LHLAAGrRGNLEIVKLLLSKGADVNARD 33
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 213-294 8.17e-03

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 37.97  E-value: 8.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 213 DGGHCSVIEWMIKDGCEVdvvdtgSGWTPLmRVSAVSGNQRVASL-----LIDAGANVNVKDRNGKTPLMVAVLNN---- 283
Cdd:PHA02716  478 DVYHCAIIERYNNAVCET------SGMTPL-HVSIISHTNANIVMdsfvyLLSIQYNINIPTKNGVTPLMLTMRNNrlsg 550

                          90
                  ....*....|..
gi 1391723754 284 -HEELVQLLLDK 294
Cdd:PHA02716  551 hQWYIVKNILDK 562
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 146-310 9.60e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 37.80  E-value: 9.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 146 AQKGYTRLVKILVSNGTDVNLKNGSGKDSLMLACYAGHLDVVKYLRrhgaswqardlggctalhwaadgghcsvieWMIK 225
Cdd:PHA02989   83 TSNKIKKIVKLLLKFGADINLKTFNGVSPIVCFIYNSNINNCDMLR------------------------------FLLS 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723754 226 DGCEVDVVDTGSGWTPL-MRVSAVSGNQRVASLLIDAGANV-NVKDRNGKTPLMVAVLNNHE----ELVQLLLDKGADAS 299
Cdd:PHA02989  133 KGINVNDVKNSRGYNLLhMYLESFSVKKDVIKILLSFGVNLfEKTSLYGLTPMNIYLRNDIDvisiKVIKYLIKKGVNIE 212

                         170
                  ....*....|.
gi 1391723754 300 VKNEFGKGVLE 310
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH