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Conserved domains on  [gi|2201823159|ref|XP_046790906|]
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ankyrin repeat family A protein 2 isoform X1 [Gallus gallus]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 15722433)

ankyrin repeat (ANK) domain-containing protein is involved in mediating protein-protein interactions

CATH:  1.25.40.20
Gene Ontology:  GO:0005515
PubMed:  15152081|17176038
SCOP:  3000154

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
169-313 4.22e-42

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 147.02  E-value: 4.22e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823159 169 IEQENVINHKDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQILGKGRESALSLACSKGYTDIVKMLLDCGVDVNEYDWNG 248
Cdd:COG0666   107 LEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDG 186

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2201823159 249 GTPLLYAVHGNHVKCVKILLESGADPTIETDAGYNSMDLAVALGYRSVQQVIESHLLKLLQSIKE 313
Cdd:COG0666   187 ETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKD 251
PHA03100 super family cl39094
ankyrin repeat protein; Provisional
 53-282 2.36e-04

ankyrin repeat protein; Provisional


The actual alignment was detected with superfamily member PHA02878:

Pssm-ID: 476869 [Multi-domain]  Cd Length: 477  Bit Score: 42.56  E-value: 2.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823159  53 KFILPNRFDMNVCSRFVkslnEEDSKNIQDQVnsDLEVASVLFK--AECNIHTspspgiqvRHvyTPSTTKHFSPIKQST 130
Cdd:PHA02878  118 KIILTNRYKNIQTIDLV----YIDKKSKDDII--EAEITKLLLSygADINMKD--------RH--KGNTALHYATENKDQ 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823159 131 TLTNK--HRGNEVSTtPLLVNSLSVHQLAAQGEMLYLATRIEQENVINHKDEEGFTPLMWAAAH-GQIAVVEFLLQNGAD 207
Cdd:PHA02878  182 RLTELllSYGANVNI-PDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVD 260

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823159 208 ----PQILGKgreSALSLACSKgyTDIVKMLLDCGVDVNEYDWNGGTPLLYAVHGNH-VKCVKIL-----LESGADPTIE 277
Cdd:PHA02878  261 vnakSYILGL---TALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSAVKQYLcINIGRILisnicLLKRIKPDIK 335


                  ....*
gi 2201823159 278 TDAGY 282
Cdd:PHA02878  336 NSEGF 340
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
169-313 4.22e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 147.02  E-value: 4.22e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823159 169 IEQENVINHKDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQILGKGRESALSLACSKGYTDIVKMLLDCGVDVNEYDWNG 248
Cdd:COG0666   107 LEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDG 186

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2201823159 249 GTPLLYAVHGNHVKCVKILLESGADPTIETDAGYNSMDLAVALGYRSVQQVIESHLLKLLQSIKE 313
Cdd:COG0666   187 ETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKD 251
Ank_2 pfam12796
Ankyrin repeats (3 copies);
186-276 7.92e-24

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.87  E-value: 7.92e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823159 186 LMWAAAHGQIAVVEFLLQNGADPQILGKGRESALSLACSKGYTDIVKMLLDCgVDVNEYDwNGGTPLLYAVHGNHVKCVK 265
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|.
gi 2201823159 266 ILLESGADPTI 276
Cdd:pfam12796  79 LLLEKGADINV 89
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 175-290 6.07e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 74.70  E-value: 6.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823159 175 INHKDEEGFTPLMWAAAH--GQIAVVEFLLQNGADPQILGKGRESALSLA--CSKGYTDIVKMLLDCGVDVN-----EY- 244
Cdd:PHA03100   99 VNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYleSNKIDLKILKLLIDKGVDINaknrvNYl 178

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2201823159 245 ----------DWNGGTPLLYAVHGNHVKCVKILLESGADPTIETDAGYNSMDLAVA 290
Cdd:PHA03100  179 lsygvpinikDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAIL 234
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 181-208 6.75e-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: 42.19  E-value: 6.75e-06
                           10        20
                   ....*....|....*....|....*...
gi 2201823159  181 EGFTPLMWAAAHGQIAVVEFLLQNGADP 208
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 53-282 2.36e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 42.56  E-value: 2.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823159  53 KFILPNRFDMNVCSRFVkslnEEDSKNIQDQVnsDLEVASVLFK--AECNIHTspspgiqvRHvyTPSTTKHFSPIKQST 130
Cdd:PHA02878  118 KIILTNRYKNIQTIDLV----YIDKKSKDDII--EAEITKLLLSygADINMKD--------RH--KGNTALHYATENKDQ 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823159 131 TLTNK--HRGNEVSTtPLLVNSLSVHQLAAQGEMLYLATRIEQENVINHKDEEGFTPLMWAAAH-GQIAVVEFLLQNGAD 207
Cdd:PHA02878  182 RLTELllSYGANVNI-PDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVD 260

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823159 208 ----PQILGKgreSALSLACSKgyTDIVKMLLDCGVDVNEYDWNGGTPLLYAVHGNH-VKCVKIL-----LESGADPTIE 277
Cdd:PHA02878  261 vnakSYILGL---TALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSAVKQYLcINIGRILisnicLLKRIKPDIK 335


                  ....*
gi 2201823159 278 TDAGY 282
Cdd:PHA02878  336 NSEGF 340
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 181-252 3.62e-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: 3.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823159 181 EGFTPLMWAAAHGQIAVVEFLLQNGAD---PQILG----KGR-------ESALSLACSKGYTDIVKMLLDCGVDVNEYDW 246
Cdd:cd22192    88 QGETALHIAVVNQNLNLVRELIARGADvvsPRATGtffrPGPknliyygEHPLSFAACVGNEEIVRLLIEHGADIRAQDS 167


                  ....*.
gi 2201823159 247 NGGTPL 252
Cdd:cd22192   168 LGNTVL 173
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 157-273 1.23e-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: 40.45  E-value: 1.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823159 157 AAQGEMLYLATRIEQENV---INHKDEEGFTPLMWAAAHGQ-IAVVEFLLQNGADPQIlGKgresALSLACSKGYTDIVK 232
Cdd:TIGR00870  24 AAERGDLASVYRDLEEPKklnINCPDRLGRSALFVAAIENEnLELTELLLNLSCRGAV-GD----TLLHAISLEYVDAVE 98

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2201823159 233 MLL----------DCGVDVNEYDWN----GGTPLLYAVHGNHVKCVKILLESGAD 273
Cdd:TIGR00870  99 AILlhllaafrksGPLELANDQYTSeftpGITALHLAAHRQNYEIVKLLLERGAS 153
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
169-313 4.22e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 147.02  E-value: 4.22e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823159 169 IEQENVINHKDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQILGKGRESALSLACSKGYTDIVKMLLDCGVDVNEYDWNG 248
Cdd:COG0666   107 LEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDG 186

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2201823159 249 GTPLLYAVHGNHVKCVKILLESGADPTIETDAGYNSMDLAVALGYRSVQQVIESHLLKLLQSIKE 313
Cdd:COG0666   187 ETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKD 251
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
154-293 4.35e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 128.92  E-value: 4.35e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823159 154 HQLAAQGEMLYLATRIEQENVINHKDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQILGKGRESALSLACSKGYTDIVKM 233
Cdd:COG0666    59 LAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKL 138

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823159 234 LLDCGVDVNEYDWNGGTPLLYAVHGNHVKCVKILLESGADPTIETDAGYNSMDLAVALGY 293
Cdd:COG0666   139 LLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGH 198
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
175-294 9.16e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 122.76  E-value: 9.16e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823159 175 INHKDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQILGKGRESALSLACSKGYTDIVKMLLDCGVDVNEYDWNGGTPLLY 254
Cdd:COG0666   146 VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDL 225

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2201823159 255 AVHGNHVKCVKILLESGADPTIETDAGYNSMDLAVALGYR 294
Cdd:COG0666   226 AAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAA 265
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
146-293 5.26e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 98.87  E-value: 5.26e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823159 146 LLVNSLSVHQLAAQGEMLYLATRIEQENVINHKDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQILGKGRESALSLACSK 225
Cdd:COG0666    18 LLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARN 97

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2201823159 226 GYTDIVKMLLDCGVDVNEYDWNGGTPLLYAVHGNHVKCVKILLESGADPTIETDAGYNSMDLAVALGY 293
Cdd:COG0666    98 GDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165
Ank_2 pfam12796
Ankyrin repeats (3 copies);
186-276 7.92e-24

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.87  E-value: 7.92e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823159 186 LMWAAAHGQIAVVEFLLQNGADPQILGKGRESALSLACSKGYTDIVKMLLDCgVDVNEYDwNGGTPLLYAVHGNHVKCVK 265
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|.
gi 2201823159 266 ILLESGADPTI 276
Cdd:pfam12796  79 LLLEKGADINV 89
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
175-283 5.74e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 90.78  E-value: 5.74e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823159 175 INHKDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQILGKGRESALSLACSKGYTDIVKMLLDCGVDVNEYDWNGGTPLLY 254
Cdd:COG0666   179 VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLL 258

                          90       100
                  ....*....|....*....|....*....
gi 2201823159 255 AVHGNHVKCVKILLESGADPTIETDAGYN 283
Cdd:COG0666   259 AAAAGAALIVKLLLLALLLLAAALLDLLT 287
Ank_2 pfam12796
Ankyrin repeats (3 copies);
156-245 1.31e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.92  E-value: 1.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823159 156 LAAQGEMLYLATR-IEQENVINHKDEEGFTPLMWAAAHGQIAVVEFLLQNgADPQILGKGReSALSLACSKGYTDIVKML 234
Cdd:pfam12796   3 LAAKNGNLELVKLlLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGR-TALHYAARSGHLEIVKLL 80

                          90
                  ....*....|.
gi 2201823159 235 LDCGVDVNEYD 245
Cdd:pfam12796  81 LEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 175-290 6.07e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 74.70  E-value: 6.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823159 175 INHKDEEGFTPLMWAAAH--GQIAVVEFLLQNGADPQILGKGRESALSLA--CSKGYTDIVKMLLDCGVDVN-----EY- 244
Cdd:PHA03100   99 VNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYleSNKIDLKILKLLIDKGVDINaknrvNYl 178

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2201823159 245 ----------DWNGGTPLLYAVHGNHVKCVKILLESGADPTIETDAGYNSMDLAVA 290
Cdd:PHA03100  179 lsygvpinikDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAIL 234
Ank_2 pfam12796
Ankyrin repeats (3 copies);
219-296 4.81e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 66.68  E-value: 4.81e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2201823159 219 LSLACSKGYTDIVKMLLDCGVDVNEYDWNGGTPLLYAVHGNHVKCVKILLESgADPTIeTDAGYNSMDLAVALGYRSV 296
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNL-KDNGRTALHYAARSGHLEI 76
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
162-296 3.82e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 62.66  E-value: 3.82e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823159 162 MLYLATRIEQENVINHKDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQILGKGRESALSLACSKGYTDIVKMLLDCGVDV 241
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2201823159 242 NEYDWNGGTPLLYAVHGNHVKCVKILLESGADPTIETDAGYNSMDLAVALGYRSV 296
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI 135
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 169-308 6.82e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 62.76  E-value: 6.82e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823159 169 IEQENVINHKDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQILGKGRESALSLACSKGYT-----DIVKMLLDCGVDVNE 243
Cdd:PHA03100   22 IMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNA 101

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2201823159 244 YDWNGGTPLLYAV--HGNHVKCVKILLESGADPTIETDAGYNSMDLAVALGYrsvqqvIESHLLKLL 308
Cdd:PHA03100  102 PDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNK------IDLKILKLL 162
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 173-289 1.02e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 62.29  E-value: 1.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823159 173 NVINHKDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQILGKGRESALSLACSKGYTDIVKML------------------ 234
Cdd:PHA02874   26 NCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLidngvdtsilpipciekd 105

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823159 235 -----LDCGVDVNEYDWNGGTPLLYAVHGNHVKCVKILLESGADPTIETDAGYNSMDLAV 289
Cdd:PHA02874  106 miktiLDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAI 165
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 180-274 5.07e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 60.00  E-value: 5.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823159 180 EEGFTPLMWAAAHGQIAVVEFLLQNGADPQILGKGRESALSLACSKGYTDIVKMLLDCGVDVNEYDWNGGTPLLYAVHGN 259
Cdd:PHA02875  100 KDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKG 179

                          90
                  ....*....|....*
gi 2201823159 260 HVKCVKILLESGADP 274
Cdd:PHA02875  180 DIAICKMLLDSGANI 194
Ank_4 pfam13637
Ankyrin repeats (many copies);
215-268 1.03e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.43  E-value: 1.03e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2201823159 215 RESALSLACSKGYTDIVKMLLDCGVDVNEYDWNGGTPLLYAVHGNHVKCVKILL 268
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 231-303 2.30e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 58.37  E-value: 2.30e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2201823159 231 VKMLLDCGVDVNEYDWNGGTPLLYAVHGNHVKCVKILLESGADPTIETDAGYNSMDLAVALGYRSVQQVIESH 303
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 175-296 2.42e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 58.05  E-value: 2.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823159 175 INHKDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQILGKGRESALSLACSKGYTDIVKMLLDCGVDVNEYDWNGGTPLLY 254
Cdd:PHA02874  117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2201823159 255 AVHGNHVKCVKILLESGADPTIETDAGYNSMDLAVaLGYRSV 296
Cdd:PHA02874  197 AAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI-IHNRSA 237
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 175-278 3.53e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 57.58  E-value: 3.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823159 175 INHKDEE-GFTPLMWAAAHGQIAVVEFLLQNGADPQILGKGRESALSLACSKGYTDIVKMLLDCGVDVNEYDWNGGTPLL 253
Cdd:PHA02878  160 INMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLH 239

                          90       100
                  ....*....|....*....|....*.
gi 2201823159 254 YAV-HGNHVKCVKILLESGADPTIET 278
Cdd:PHA02878  240 ISVgYCKDYDILKLLLEHGVDVNAKS 265
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 175-242 5.02e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 56.98  E-value: 5.02e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2201823159 175 INHKDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQILGKGRESALSLACSKGYTDIVKMLLDCGVDVN 242
Cdd:PHA03100  185 INIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
PHA03095 PHA03095
ankyrin-like protein; Provisional
 175-308 5.37e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 56.96  E-value: 5.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823159 175 INHKDEEGFTPL---MWAAAHGQIAVVEFLLQNGAD---PQILGKgreSAL-SLACSKGYTDIVKMLLDCGVDVNEYDWN 247
Cdd:PHA03095   40 VNFRGEYGKTPLhlyLHYSSEKVKDIVRLLLEAGADvnaPERCGF---TPLhLYLYNATTLDVIKLLIKAGADVNAKDKV 116

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2201823159 248 GGTPL-LYAVHGN-HVKCVKILLESGADPTIETDAGYNSMDLAValgyRSVQQVIEshLLKLL 308
Cdd:PHA03095  117 GRTPLhVYLSGFNiNPKVIRLLLRKGADVNALDLYGMTPLAVLL----KSRNANVE--LLRLL 173
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 175-300 1.39e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 55.84  E-value: 1.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823159 175 INHKDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQILGKGRESALSLA-CSKGYTDIVKMLLDCGVDVNEYDWNGGTPLL 253
Cdd:PHA02876  368 VNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLH 447

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2201823159 254 YAVHGN-HVKCVKILLESGADptIETDAGYNSMDLAVALGYRSVQQVI 300
Cdd:PHA02876  448 YACKKNcKLDVIEMLLDNGAD--VNAINIQNQYPLLIALEYHGIVNIL 493
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 172-279 1.77e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 55.64  E-value: 1.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823159 172 ENVINHKDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQIL-GKGReSALSLACSKGYTDIVKMLLDCGVDVNEYDWNGGT 250
Cdd:PLN03192  515 DNGGEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGdSKGR-TPLHIAASKGYEDCVLVLLKHACNVHIRDANGNT 593

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2201823159 251 PLLYAVHGNHVKCVKIL--LESGADPTIETD 279
Cdd:PLN03192  594 ALWNAISAKHHKIFRILyhFASISDPHAAGD 624
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 140-248 2.22e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 55.29  E-value: 2.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823159 140 EVSTTPLLVNSLSVH--QLAAQGEMLYLATRIEQENVINHKDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQILGKGRES 217
Cdd:PTZ00322   71 EEVIDPVVAHMLTVElcQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKT 150

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2201823159 218 ALSLACSKGYTDIVKMLLDCGVDVNEYDWNG 248
Cdd:PTZ00322  151 PLELAEENGFREVVQLLSRHSQCHFELGANA 181
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 175-301 4.44e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 54.20  E-value: 4.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823159 175 INHKDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQILG---------------------KGRESA--LSLACSKGYTDIV 231
Cdd:PHA02874   61 INHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSILPipciekdmiktildcgidvniKDAELKtfLHYAIKKGDLESI 140

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2201823159 232 KMLLDCGVDVNEYDWNGGTPLLYAVHGNHVKCVKILLESGADPTIETDAGYNSMDLAVALG-YRSVQQVIE 301
Cdd:PHA02874  141 KMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGdYACIKLLID 211
Ank_4 pfam13637
Ankyrin repeats (many copies);
184-235 8.22e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.04  E-value: 8.22e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2201823159 184 TPLMWAAAHGQIAVVEFLLQNGADPQILGKGRESALSLACSKGYTDIVKMLL 235
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 176-292 8.57e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 53.07  E-value: 8.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823159 176 NHKDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQILGKGRESALSLACSKGYTDIVKMLLDCGVDVNEYDW-NGGTPLLY 254
Cdd:PHA02875   29 NFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYkDGMTPLHL 108

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2201823159 255 AVHGNHVKCVKILLESGADPTIETDAGYNSMDLAVALG 292
Cdd:PHA02875  109 ATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMG 146
Ank_5 pfam13857
Ankyrin repeats (many copies);
201-255 9.51e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.11  E-value: 9.51e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2201823159 201 LLQNG-ADPQILGKGRESALSLACSKGYTDIVKMLLDCGVDVNEYDWNGGTPLLYA 255
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 163-278 1.06e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 52.69  E-value: 1.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823159 163 LYLATRIEQENVI----------NHKDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQILGKGRESALSLACSKGYTDIVK 232
Cdd:PHA02875  106 LHLATILKKLDIMklliargadpDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICK 185

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2201823159 233 MLLDCGVDVNEYDWNGGTPLL-YAVHGNHVKCVKILLESGADPTIET 278
Cdd:PHA02875  186 MLLDSGANIDYFGKNGCVAALcYAIENNKIDIVRLFIKRGADCNIMF 232
PHA03095 PHA03095
ankyrin-like protein; Provisional
 196-290 2.60e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 51.56  E-value: 2.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823159 196 AVVEFLLQNGADP---QILGKGRESALSLACSKGYTDIVKMLLDcGVDVNEYDWNGGTPLLYA-VHGNHVKCVKiLLESG 271
Cdd:PHA03095  203 RIVRELIRAGCDPaatDMLGNTPLHSMATGSSCKRSLVLPLLIA-GISINARNRYGQTPLHYAaVFNNPRACRR-LIALG 280

                          90
                  ....*....|....*....
gi 2201823159 272 ADPTIETDAGYNSMDLAVA 290
Cdd:PHA03095  281 ADINAVSSDGNTPLSLMVR 299
Ank_2 pfam12796
Ankyrin repeats (3 copies);
146-210 4.81e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 47.03  E-value: 4.81e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2201823159 146 LLVNSLSVHQLAAQGEM-LYLATRIEQENV----INHKD----EEGFTPLMWAAAHGQIAVVEFLLQNGADPQI 210
Cdd:pfam12796  16 LLENGADANLQDKNGRTaLHLAAKNGHLEIvkllLEHADvnlkDNGRTALHYAARSGHLEIVKLLLEKGADINV 89
Ank_5 pfam13857
Ankyrin repeats (many copies);
175-222 7.22e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.42  E-value: 7.22e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2201823159 175 INHKDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQILGKGRESALSLA 222
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
169-252 7.80e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 49.57  E-value: 7.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823159 169 IEQENVINHKDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQILGKGRESALSLACSKGYTDIVKMLLDCGVDVNEYDWNG 248
Cdd:COG0666   206 LEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285


                  ....
gi 2201823159 249 GTPL 252
Cdd:COG0666   286 LTLL 289
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 198-278 1.09e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 49.66  E-value: 1.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823159 198 VEFLLQNGADPQILGKGRESALSLACSKGYTDIVKMLLDCGVDVNEYDWNGGTPLLYAVHGNHVKCVKILLESGadPTIE 277
Cdd:PHA03100  175 VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNG--PSIK 252


                  .
gi 2201823159 278 T 278
Cdd:PHA03100  253 T 253
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 169-288 1.96e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 48.81  E-value: 1.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823159 169 IEQENVINHKDEEGFTPLMWAAAHGQIAVVEFLLQNGadpqilgkgreSALSLACSKGYT----------DIVKMLLDcG 238
Cdd:PHA02874  177 LEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHG-----------NHIMNKCKNGFTplhnaiihnrSAIELLIN-N 244

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2201823159 239 VDVNEYDWNGGTPLLYAVHGN-HVKCVKILLESGADPTIETDAGYNSMDLA 288
Cdd:PHA02874  245 ASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTA 295
Ank_5 pfam13857
Ankyrin repeats (many copies);
234-288 4.91e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.10  E-value: 4.91e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2201823159 234 LLDCG-VDVNEYDWNGGTPLLYAVHGNHVKCVKILLESGADPTIETDAGYNSMDLA 288
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 126-293 6.51e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 47.75  E-value: 6.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823159 126 IKQSTTLTNKHRGNEVSTTPLLV----NSLSVHQLAAQGE-MLYLATRIEQENV------------INHKDEEGFTPLMW 188
Cdd:PHA02876  105 IKYASIILNKHKLDEACIHILKEaisgNDIHYDKINESIEyMKLIKERIQQDELliaemlleggadVNAKDIYCITPIHY 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823159 189 AAAHGQIAVVEFLLQNGADPQILGKGRESALSLACSKGYTDIVK-----------------------------MLLDCGV 239
Cdd:PHA02876  185 AAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKaiidnrsninkndlsllkairnedletslLLYDAGF 264

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2201823159 240 DVNEYDWNGGTPLLYAVHGNHV-KCVKILLESGADPTIETDAGYNSMDLAVALGY 293
Cdd:PHA02876  265 SVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAKNGY 319
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 181-208 6.75e-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: 42.19  E-value: 6.75e-06
                           10        20
                   ....*....|....*....|....*...
gi 2201823159  181 EGFTPLMWAAAHGQIAVVEFLLQNGADP 208
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 181-210 8.15e-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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 41.86  E-value: 8.15e-06
                          10        20        30
                  ....*....|....*....|....*....|
gi 2201823159 181 EGFTPLMWAAAHGQIAVVEFLLQNGADPQI 210
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 181-213 9.20e-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: 41.89  E-value: 9.20e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2201823159 181 EGFTPLMWAAAH-GQIAVVEFLLQNGADPQILGK 213
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
Ank_4 pfam13637
Ankyrin repeats (many copies);
153-202 1.77e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.49  E-value: 1.77e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2201823159 153 VHQLAAQGEMLYLATRIEQENVINHKDEEGFTPLMWAAAHGQIAVVEFLL 202
Cdd:pfam13637   5 LHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 127-273 1.80e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.21  E-value: 1.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823159 127 KQSTTLTNKHRGNEVSTTPLL------VNSLSVHQ-----LAAQGEML--YLATRIEQENVINHKDEEGFTPLMWAAAHG 193
Cdd:PHA02876  239 KNDLSLLKAIRNEDLETSLLLydagfsVNSIDDCKntplhHASQAPSLsrLVPKLLERGADVNAKNIKGETPLYLMAKNG 318

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823159 194 -QIAVVEFLLQNGADPQILGKGRESALSLACS-KGYTDIVKMLLDCGVDVNEYDWNGGTPLLYAVHGNHVKCVKILLESG 271
Cdd:PHA02876  319 yDTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYG 398


                  ..
gi 2201823159 272 AD 273
Cdd:PHA02876  399 AD 400
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 175-300 3.81e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 45.24  E-value: 3.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823159 175 INHKDEEGFTPlMW---AAAHGQIAVVEFLLQNGADPQILGkgreSALSLACSKGYTDIVKMLLDCGVDVNEYDWNGGTP 251
Cdd:PLN03192  584 VHIRDANGNTA-LWnaiSAKHHKIFRILYHFASISDPHAAG----DLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATA 658

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2201823159 252 LLYAVHGNHVKCVKILLESGADPT-IETDAGYNSMDLAVALGYRSVQQVI 300
Cdd:PLN03192  659 LQVAMAEDHVDMVRLLIMNGADVDkANTDDDFSPTELRELLQKRELGHSI 708
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 194-283 5.78e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 44.35  E-value: 5.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823159 194 QIAVVEFLLQNGADPQILG----------KGRESAlslacSKGYTDIVKMLLDCGVDVNEYDWNGGTPL---LYAVHGNH 260
Cdd:PHA02989   49 KIKIVKLLIDNGADVNYKGyietplcavlRNREIT-----SNKIKKIVKLLLKFGADINLKTFNGVSPIvcfIYNSNINN 123

                          90       100
                  ....*....|....*....|....
gi 2201823159 261 VKCVKILLESGAD-PTIETDAGYN 283
Cdd:PHA02989  124 CDMLRFLLSKGINvNDVKNSRGYN 147
PHA03095 PHA03095
ankyrin-like protein; Provisional
 175-235 7.39e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 44.25  E-value: 7.39e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2201823159 175 INHKDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQILGKGRESALSLACSKGYTDIVKMLL 235
Cdd:PHA03095  250 INARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 197-301 7.71e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 42.88  E-value: 7.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823159 197 VVEFLLQNGADPQILGKGRE-SALS--LACSKGYT-DIVKMLLDCGVDVNEYDWNGGTPL-LYAVHGN-HVKCVKILLES 270
Cdd:PHA02859   68 ILKFLIENGADVNFKTRDNNlSALHhyLSFNKNVEpEILKILIDSGSSITEEDEDGKNLLhMYMCNFNvRINVIKLLIDS 147

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2201823159 271 GADPtIETDAGYNSMdLAVALGYRSVQQVIE 301
Cdd:PHA02859  148 GVSF-LNKDFDNNNI-LYSYILFHSDKKIFD 176
PHA02798 PHA02798
ankyrin-like protein; Provisional
 197-308 8.12e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 44.06  E-value: 8.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823159 197 VVEFLLQNGADpqILGKGRESALSLaCS--------KGYTDIVKMLLDCGVDVNEYDWNGGTPLLYAVHGNHVKCVKILL 268
Cdd:PHA02798   53 IVKLFINLGAN--VNGLDNEYSTPL-CTilsnikdyKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILL 129

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2201823159 269 ---ESGADPTIETDAGYNSMDLAVALGYRsvqqvIESHLLKLL 308
Cdd:PHA02798  130 fmiENGADTTLLDKDGFTMLQVYLQSNHH-----IDIEIIKLL 167
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 247-279 8.72e-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: 39.19  E-value: 8.72e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2201823159 247 NGGTPLLYAV-HGNHVKCVKILLESGADPTIETD 279
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 184-300 1.31e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 43.06  E-value: 1.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823159 184 TPLMWAAAHGQIAVVEFLLQNG--ADPQILGKGReSALSLACSKGYTDIVKMLLDCGVDVNEYDWNGGTPLLYAVHGNHV 261
Cdd:PHA02875   70 SELHDAVEEGDVKAVEELLDLGkfADDVFYKDGM-TPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI 148

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2201823159 262 KCVKILLESGADPTIETDAGYNSMDLAVALGYRSVQQVI 300
Cdd:PHA02875  149 KGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKML 187
PHA02792 PHA02792
ankyrin-like protein; Provisional
 197-311 2.02e-04

ankyrin-like protein; Provisional


Pssm-ID: 165155 [Multi-domain]  Cd Length: 631  Bit Score: 43.01  E-value: 2.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823159 197 VVEFLLQNGAD---------------PQILGKGRESALSLACSKGYTDivkmlldcgvDVNEYDWNGGTPLLYAVHGNHV 261
Cdd:PHA02792  354 VVEYILKNGNVvvedddniinimplfPTLSIHESDVLSILKLCKPYID----------DINKIDKHGRSILYYCIESHSV 423

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2201823159 262 KCVKILLESGADPTIETDAGYNSMDLAVALGYRSVQQVIESHlLKLLQSI 311
Cdd:PHA02792  424 SLVEWLIDNGADINITTKYGSTCIGICVILAHACIPEIAELY-IKILEII 472
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 53-282 2.36e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 42.56  E-value: 2.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823159  53 KFILPNRFDMNVCSRFVkslnEEDSKNIQDQVnsDLEVASVLFK--AECNIHTspspgiqvRHvyTPSTTKHFSPIKQST 130
Cdd:PHA02878  118 KIILTNRYKNIQTIDLV----YIDKKSKDDII--EAEITKLLLSygADINMKD--------RH--KGNTALHYATENKDQ 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823159 131 TLTNK--HRGNEVSTtPLLVNSLSVHQLAAQGEMLYLATRIEQENVINHKDEEGFTPLMWAAAH-GQIAVVEFLLQNGAD 207
Cdd:PHA02878  182 RLTELllSYGANVNI-PDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVD 260

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823159 208 ----PQILGKgreSALSLACSKgyTDIVKMLLDCGVDVNEYDWNGGTPLLYAVHGNH-VKCVKIL-----LESGADPTIE 277
Cdd:PHA02878  261 vnakSYILGL---TALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSAVKQYLcINIGRILisnicLLKRIKPDIK 335


                  ....*
gi 2201823159 278 TDAGY 282
Cdd:PHA02878  336 NSEGF 340
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 247-276 2.79e-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: 2.79e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 2201823159  247 NGGTPLLYAVHGNHVKCVKILLESGADPTI 276
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 181-252 3.62e-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: 3.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823159 181 EGFTPLMWAAAHGQIAVVEFLLQNGAD---PQILG----KGR-------ESALSLACSKGYTDIVKMLLDCGVDVNEYDW 246
Cdd:cd22192    88 QGETALHIAVVNQNLNLVRELIARGADvvsPRATGtffrPGPknliyygEHPLSFAACVGNEEIVRLLIEHGADIRAQDS 167


                  ....*.
gi 2201823159 247 NGGTPL 252
Cdd:cd22192   168 LGNTVL 173
PHA02798 PHA02798
ankyrin-like protein; Provisional
 169-242 5.04e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 41.36  E-value: 5.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823159 169 IEQENVINHKDEEGFTPLMWAAAHGQIAVVEFLL---QNGADPQILGKGRESALSLACSKGYT---DIVKMLLDCGVDVN 242
Cdd:PHA02798   96 IENGADINKKNSDGETPLYCLLSNGYINNLEILLfmiENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDIN 175
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 197-308 5.05e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 41.40  E-value: 5.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823159 197 VVEFLLQNGADPQILGKGR-ESALSLACSKGYTDIVKMLLDCGVDVNEYDWNGGTPLLYAVHGNHVKCVKILLESGADPT 275
Cdd:PHA02878  149 ITKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTD 228

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2201823159 276 IETDAGynSMDLAVALGYrsvqqVIESHLLKLL 308
Cdd:PHA02878  229 ARDKCG--NTPLHISVGY-----CKDYDILKLL 254
PHA02791 PHA02791
ankyrin-like protein; Provisional
 179-269 5.29e-04

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 41.18  E-value: 5.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823159 179 DEEGFTPLMWAAAHGQIAVVEFLLQNGADPQILGKgrESALSLACSKGYTDIVKMLLDCGVDVNEYDWNGGTPLLYAVHG 258
Cdd:PHA02791   27 DVHGHSALYYAIADNNVRLVCTLLNAGALKNLLEN--EFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDS 104

                          90
                  ....*....|.
gi 2201823159 259 NHVKCVKILLE 269
Cdd:PHA02791  105 GNMQTVKLFVK 115
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 216-243 7.52e-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: 36.47  E-value: 7.52e-04
                          10        20
                  ....*....|....*....|....*...
gi 2201823159 216 ESALSLACSKGYTDIVKMLLDCGVDVNE 243
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 184-273 1.03e-03

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 40.77  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823159 184 TPLMWAAAHGQI-AVVEFLLQNGADPQILGKGRESALSLACSKGYTDIVKMLLDCGVD-VNE------YDwnGGTPLLYA 255
Cdd:cd22192    19 SPLLLAAKENDVqAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEpmtsdlYQ--GETALHIA 96

                          90
                  ....*....|....*...
gi 2201823159 256 VHGNHVKCVKILLESGAD 273
Cdd:cd22192    97 VVNQNLNLVRELIARGAD 114
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 197-300 1.06e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 39.97  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823159 197 VVEFLLQNGADPQILGKGRESA----LSLACSKGYTDIVKMLLDCGVDVNEY-DWNGGTPLLYAVHGNHVKCVKILLESG 271
Cdd:PHA02884   48 IIDAILKLGADPEAPFPLSENSktnpLIYAIDCDNDDAAKLLIRYGADVNRYaEEAKITPLYISVLHGCLKCLEILLSYG 127

                          90       100
                  ....*....|....*....|....*....
gi 2201823159 272 ADPTIETDAGYNSMDLAVALGYRSVQQVI 300
Cdd:PHA02884  128 ADINIQTNDMVTPIELALMICNNFLAFMI 156
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 157-273 1.23e-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: 40.45  E-value: 1.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823159 157 AAQGEMLYLATRIEQENV---INHKDEEGFTPLMWAAAHGQ-IAVVEFLLQNGADPQIlGKgresALSLACSKGYTDIVK 232
Cdd:TIGR00870  24 AAERGDLASVYRDLEEPKklnINCPDRLGRSALFVAAIENEnLELTELLLNLSCRGAV-GD----TLLHAISLEYVDAVE 98

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2201823159 233 MLL----------DCGVDVNEYDWN----GGTPLLYAVHGNHVKCVKILLESGAD 273
Cdd:TIGR00870  99 AILlhllaafrksGPLELANDQYTSeftpGITALHLAAHRQNYEIVKLLLERGAS 153
PHA02798 PHA02798
ankyrin-like protein; Provisional
 179-281 1.78e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 39.82  E-value: 1.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823159 179 DEEGFTPL---MWAAAHGQIAVVEFLLQNGADPQILGKgRESALSLACSKGYT------DIVKMLLDCG----------- 238
Cdd:PHA02798  142 DKDGFTMLqvyLQSNHHIDIEIIKLLLEKGVDINTHNN-KEKYDTLHCYFKYNidridaDILKLFVDNGfiinkenkshk 220

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2201823159 239 ----------------------------VDVNEYDWNGGTPLLYAVHGNHVKCVKILLESGADPTIETDAG 281
Cdd:PHA02798  221 kkfmeylnsllydnkrfkknildfifsyIDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELG 291
Ank_4 pfam13637
Ankyrin repeats (many copies);
248-296 2.05e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 35.71  E-value: 2.05e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2201823159 248 GGTPLLYAVHGNHVKCVKILLESGADPTIETDAGYNSMDLAVALGYRSV 296
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEV 49
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 198-273 2.09e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 39.66  E-value: 2.09e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2201823159 198 VEFLLQNGADPQILGKGRESALSLACSKG-YTDIVKMLLDCGVDVNEYDWNGGTPLLYAVHGNHVkcVKILLESGAD 273
Cdd:PHA02876  425 VKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIALEYHGI--VNILLHYGAE 499
PHA03095 PHA03095
ankyrin-like protein; Provisional
 214-273 3.10e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 38.85  E-value: 3.10e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2201823159 214 GRESAL---SLACSKGYTDIVKMLLDCGVDVNEYDWNGGTPLLYAVHGNHVKCVKI---LLESGAD 273
Cdd:PHA03095   10 IMEAALydyLLNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGAD 75
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 217-243 3.80e-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: 34.49  E-value: 3.80e-03
                           10        20
                   ....*....|....*....|....*..
gi 2201823159  217 SALSLACSKGYTDIVKMLLDCGVDVNE 243
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 93-207 3.83e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 39.08  E-value: 3.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823159  93 VLFKAECNIHTSPSPGIQVrhVYTPSTTKH---FSPIKQSTTLTNKHRGNEVSTTPLLVNSLSVHQlaaqgEMLYLATRI 169
Cdd:PLN03192  576 VLLKHACNVHIRDANGNTA--LWNAISAKHhkiFRILYHFASISDPHAAGDLLCTAAKRNDLTAMK-----ELLKQGLNV 648

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2201823159 170 EQEnvinhkDEEGFTPLMWAAAHGQIAVVEFLLQNGAD 207
Cdd:PLN03192  649 DSE------DHQGATALQVAMAEDHVDMVRLLIMNGAD 680
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 216-245 4.20e-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: 4.20e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2201823159 216 ESALSLACSK-GYTDIVKMLLDCGVDVNEYD 245
Cdd:pfam00023   3 NTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 247-276 4.78e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.16  E-value: 4.78e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 2201823159 247 NGGTPLLYAVHGNHVKCVKILLESGADPTI 276
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 139-306 5.40e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 38.59  E-value: 5.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823159 139 NEVSTTPLLVNSLsvhqLAAQGEMLYLATRIEQEnvINHKDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQILGKGR--- 215
Cdd:cd22194   104 NINENTKEIVRIL----LAFAEENGILDRFINAE--YTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVffn 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823159 216 -----------ESALSLACSKGYTDIVKMLLD-CGVDVNEYDWNGGTpLLYAV---------HGNHVKCV--KILLESGA 272
Cdd:cd22194   178 pkykhegfyfgETPLALAACTNQPEIVQLLMEkESTDITSQDSRGNT-VLHALvtvaedsktQNDFVKRMydMILLKSEN 256

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2201823159 273 D--PTIETDAGYNSMDLAVALGYRSVQQVIESHLLK 306
Cdd:cd22194   257 KnlETIRNNEGLTPLQLAAKMGKAEILKYILSREIK 292
PHA02795 PHA02795
ankyrin-like protein; Provisional
 229-308 9.51e-03

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 37.28  E-value: 9.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823159 229 DIVKMLLDCGVDVNEYDWNGGTPLLYAVHGNHVKCVKILLESGADPTIETDAGYNSMDLAVALGYRSVQQVIESHLLKLL 308
Cdd:PHA02795  202 EIYKLCIPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRGSVIARRETHLKILEIL 281
 
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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