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Conserved domains on  [gi|119606310|gb|EAW85904|]
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ankyrin repeat domain 30A [Homo sapiens]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 11429852)

ankyrin repeat domain-containing protein; ANK proteins mediate specific protein-protein interactions without necessarily recognizing specific primary sequences which allows for one ankyrin repeat domain to recognize and bind to a variety of intracellular substrates and may be involved in a wide array of functions

Gene Ontology:  GO:0005515
PubMed:  17176038
SCOP:  4000366

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
42-272 1.49e-42

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 155.88  E-value: 1.49e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310  42 IHKAASRGQVRKLEKMTKRKKTINLNIQDAQKRTALHWACVNGHEEVVTFLVDRKCQLDVLDGEHRTPLMKALQCHQEAC 121
Cdd:COG0666   56 LLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310 122 ANILIDSGADINLVDVYGNTALHYAVYSEILSVVAKLLSHGAVIEVHNKASLTPLLLSITKRSEQIVEFLLIKNANANAV 201
Cdd:COG0666  136 VKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAK 215

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119606310 202 NKYKCTALMLAVCHGSSEIVGMLLQQNVDVFAADICGVTAEHYAVTCGFHHIHEQIMEYIRKLSKNHQNTN 272
Cdd:COG0666  216 DNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLL 286
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
42-272 1.49e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 155.88  E-value: 1.49e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310  42 IHKAASRGQVRKLEKMTKRKKTINLNIQDAQKRTALHWACVNGHEEVVTFLVDRKCQLDVLDGEHRTPLMKALQCHQEAC 121
Cdd:COG0666   56 LLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310 122 ANILIDSGADINLVDVYGNTALHYAVYSEILSVVAKLLSHGAVIEVHNKASLTPLLLSITKRSEQIVEFLLIKNANANAV 201
Cdd:COG0666  136 VKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAK 215

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119606310 202 NKYKCTALMLAVCHGSSEIVGMLLQQNVDVFAADICGVTAEHYAVTCGFHHIHEQIMEYIRKLSKNHQNTN 272
Cdd:COG0666  216 DNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLL 286
Ank_2 pfam12796
Ankyrin repeats (3 copies);
77-169 2.03e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.55  E-value: 2.03e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310   77 LHWACVNGHEEVVTFLVDRKCQLDVLDGEHRTPLMKALQCHQEACANILIDSgADINLVDvYGNTALHYAVYSEILSVVA 156
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 119606310  157 KLLSHGAVIEVHN 169
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 65-213 6.38e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 84.16  E-value: 6.38e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310  65 NLNIQDAQK-RTALHWACVNGHEEVVTFLVDRKCQLDVLDGEHRTPLMKALQCHQEACANILIDSGADINLVDVYGNTAL 143
Cdd:PHA02878 159 DINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPL 238

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119606310 144 HYAVYSEI-LSVVAKLLSHGAviEVHNKAS---LTPLLLSItkRSEQIVEFLLIKNANANAVNKYKCTALMLAV 213
Cdd:PHA02878 239 HISVGYCKdYDILKLLLEHGV--DVNAKSYilgLTALHSSI--KSERKLKLLLEYGADINSLNSYKLTPLSSAV 308
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 72-194 1.78e-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: 51.17  E-value: 1.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310  72 QKRTALHWACVNGHEEVV-----------------TFLVDRKCQLdVLDGEHrtPLMKALQCHQEACANILIDSGADINL 134
Cdd:cd22192   88 QGETALHIAVVNQNLNLVreliargadvvspratgTFFRPGPKNL-IYYGEH--PLSFAACVGNEEIVRLLIEHGADIRA 164

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119606310 135 VDVYGNTALHYAV-----------YSEILSVVAKLLSHgAVIEVHNKASLTPLLLSITKRSEQIVEFLLIK 194
Cdd:cd22192  165 QDSLGNTVLHILVlqpnktfacqmYDLILSYDKEDDLQ-PLDLVPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 72-101 7.28e-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: 7.28e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 119606310    72 QKRTALHWACVNGHEEVVTFLVDRKCQLDV 101
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 131-251 7.94e-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: 39.68  E-value: 7.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310  131 DINLVDVYGNTAL-HYAVYSEILSVVAKLLSHGAVIEVhNKAsltpLLLSITKRSEQIVE-FLLIKNANAN-------AV 201
Cdd:TIGR00870  44 NINCPDRLGRSALfVAAIENENLELTELLLNLSCRGAV-GDT----LLHAISLEYVDAVEaILLHLLAAFRksgplelAN 118

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 119606310  202 NKYKC------TALMLAVCHGSSEIVGMLLQQNVDVFAADICGVTAEHYAVTCGFH 251
Cdd:TIGR00870 119 DQYTSeftpgiTALHLAAHRQNYEIVKLLLERGASVPARACGDFFVKSQGVDSFYH 174
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
42-272 1.49e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 155.88  E-value: 1.49e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310  42 IHKAASRGQVRKLEKMTKRKKTINLNIQDAQKRTALHWACVNGHEEVVTFLVDRKCQLDVLDGEHRTPLMKALQCHQEAC 121
Cdd:COG0666   56 LLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310 122 ANILIDSGADINLVDVYGNTALHYAVYSEILSVVAKLLSHGAVIEVHNKASLTPLLLSITKRSEQIVEFLLIKNANANAV 201
Cdd:COG0666  136 VKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAK 215

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119606310 202 NKYKCTALMLAVCHGSSEIVGMLLQQNVDVFAADICGVTAEHYAVTCGFHHIHEQIMEYIRKLSKNHQNTN 272
Cdd:COG0666  216 DNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLL 286
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
29-272 1.30e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 153.19  E-value: 1.30e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310  29 NDSYIVHSGDLRKIHKAASRGQVRKLEKMTKRKKTINLNIQDAQKRTALHWACVNGHEEVVTFLVDRKCQLDVLDGEHRT 108
Cdd:COG0666   10 LLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNT 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310 109 PLMKALQCHQEACANILIDSGADINLVDVYGNTALHYAVYSEILSVVAKLLSHGAVIEVHNKASLTPLLLSITKRSEQIV 188
Cdd:COG0666   90 LLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310 189 EFLLIKNANANAVNKYKCTALMLAVCHGSSEIVGMLLQQNVDVFAADICGVTAEHYAVTCGFHHIHEQIMEYIRKLSKNH 268
Cdd:COG0666  170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKD 249


                 ....
gi 119606310 269 QNTN 272
Cdd:COG0666  250 KDGL 253
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
61-333 3.09e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 120.83  E-value: 3.09e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310  61 KKTINLNIQDAQKRTALHWACVNGHEEVVTFLVDRKCQLDVLDGEHRTPLMKALQCHQEACANILIDSGADINLVDVYGN 140
Cdd:COG0666    9 LLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGN 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310 141 TALHYAVYSEILSVVAKLLSHGAVIEVHNKASLTPLLLSITKRSEQIVEFLLIKNANANAVNKYKCTALMLAVCHGSSEI 220
Cdd:COG0666   89 TLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEI 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310 221 VGMLLQQNVDVFAADICGVTAEHYAVTCGfhhiHEQIMEYIRKLSKNHQNTNPEGTSAgtPDEAAplAERTPDTAESLVE 300
Cdd:COG0666  169 VKLLLEAGADVNARDNDGETPLHLAAENG----HLEIVKLLLEAGADVNAKDNDGKTA--LDLAA--ENGNLEIVKLLLE 240

                        250       260       270
                 ....*....|....*....|....*....|...
gi 119606310 301 KTPDEAAPLVERTPDTAESLVEKTPDEAASLVE 333
Cdd:COG0666  241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLL 273
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
42-209 3.56e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 120.83  E-value: 3.56e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310  42 IHKAASRGQVRKLEKMTKRKktINLNIQDAQKRTALHWACVNGHEEVVTFLVDRKCQLDVLDGEHRTPLMKALQCHQEAC 121
Cdd:COG0666  124 LHLAAYNGNLEIVKLLLEAG--ADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEI 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310 122 ANILIDSGADINLVDVYGNTALHYAVYSEILSVVAKLLSHGAVIEVHNKASLTPLLLSITKRSEQIVEFLLIKNANANAV 201
Cdd:COG0666  202 VKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAA 281


                 ....*...
gi 119606310 202 NKYKCTAL 209
Cdd:COG0666  282 LLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
77-169 2.03e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.55  E-value: 2.03e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310   77 LHWACVNGHEEVVTFLVDRKCQLDVLDGEHRTPLMKALQCHQEACANILIDSgADINLVDvYGNTALHYAVYSEILSVVA 156
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 119606310  157 KLLSHGAVIEVHN 169
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
42-136 1.66e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.85  E-value: 1.66e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310   42 IHKAASRGQVRKLEKMTKRKktINLNIQDAQKRTALHWACVNGHEEVVTFLVDRKCQLDVLDGehRTPLMKALQCHQEAC 121
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENG--ADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNG--RTALHYAARSGHLEI 76

                          90
                  ....*....|....*
gi 119606310  122 ANILIDSGADINLVD 136
Cdd:pfam12796  77 VKLLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 65-213 6.38e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 84.16  E-value: 6.38e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310  65 NLNIQDAQK-RTALHWACVNGHEEVVTFLVDRKCQLDVLDGEHRTPLMKALQCHQEACANILIDSGADINLVDVYGNTAL 143
Cdd:PHA02878 159 DINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPL 238

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119606310 144 HYAVYSEI-LSVVAKLLSHGAviEVHNKAS---LTPLLLSItkRSEQIVEFLLIKNANANAVNKYKCTALMLAV 213
Cdd:PHA02878 239 HISVGYCKdYDILKLLLEHGV--DVNAKSYilgLTALHSSI--KSERKLKLLLEYGADINSLNSYKLTPLSSAV 308
PHA03095 PHA03095
ankyrin-like protein; Provisional
 103-292 2.65e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 81.99  E-value: 2.65e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310 103 DGEH-RTPLMKALQCHQEACANI---LIDSGADINLVDVYGNTALH-YAVYSEILSVVAKLLSHGAVIEVHNKASLTPL- 176
Cdd:PHA03095  43 RGEYgKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLh 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310 177 -LLSITKRSEQIVEFLLIKNANANAVNKYKCTAL-MLAVCHGSS-EIVGMLLQQNVDVFAADICGVTAehyavtcgFHHI 253
Cdd:PHA03095 123 vYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLaVLLKSRNANvELLRLLIDAGADVYAVDDRFRSL--------LHHH 194

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 119606310 254 HEQIMEYIRKLSKNhqntnpegTSAGTPDEAAPLAERTP 292
Cdd:PHA03095 195 LQSFKPRARIVREL--------IRAGCDPAATDMLGNTP 225
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 92-246 4.78e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 80.86  E-value: 4.78e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310  92 LVDRKCQLDVLDGEHRTPLMKALQCHQEACANILIDSGADINLVDVYGNTALHY-----AVYSEILSVVAKLLSHGAVIE 166
Cdd:PHA03100  21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYlsnikYNLTDVKEIVKLLLEYGANVN 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310 167 VHNKASLTPLLLSITKRSEQ--IVEFLLIKNANANAVNKYKCTALMLAV--CHGSSEIVGMLLQQNVDVFA--------- 233
Cdd:PHA03100 101 APDNNGITPLLYAISKKSNSysIVEYLLDNGANVNIKNSDGENLLHLYLesNKIDLKILKLLIDKGVDINAknrvnylls 180

                        170       180
                 ....*....|....*....|
gi 119606310 234 -------ADICGVTAEHYAV 246
Cdd:PHA03100 181 ygvpiniKDVYGFTPLHYAV 200
Ank_2 pfam12796
Ankyrin repeats (3 copies);
143-235 3.04e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 71.69  E-value: 3.04e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310  143 LHYAVYSEILSVVAKLLSHGAVIEVHNKASLTPLLLSITKRSEQIVEfLLIKNANANAVNkYKCTALMLAVCHGSSEIVG 222
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVK-LLLEHADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 119606310  223 MLLQQNVDVFAAD 235
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 61-241 1.45e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 73.52  E-value: 1.45e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310  61 KKTINLNIQDAQKRTALHwACVNG---HEEVVTFLVDRKCQLDVLDGEHRTPLMKALQCHqEACA---NILIDSGADINL 134
Cdd:PHA03095 105 KAGADVNAKDKVGRTPLH-VYLSGfniNPKVIRLLLRKGADVNALDLYGMTPLAVLLKSR-NANVellRLLIDAGADVYA 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310 135 VDVYGNTALHY-AVYSEI-LSVVAKLLSHGAVIEVHNKASLTPLLLSITKRSEQ--IVEFLLIKNANANAVNKYKCTALM 210
Cdd:PHA03095 183 VDDRFRSLLHHhLQSFKPrARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPLH 262

                        170       180       190
                 ....*....|....*....|....*....|.
gi 119606310 211 LAVCHGSSEIVGMLLQQNVDVFAADICGVTA 241
Cdd:PHA03095 263 YAAVFNNPRACRRLIALGADINAVSSDGNTP 293
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 64-204 3.18e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 72.39  E-value: 3.18e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310  64 INLNIQDAQKRTALHWACVNGHE--EVVTFLVDRKCQLDVLDGehrtplmkalqchqeacANILIDSGADINLVDVYGNT 141
Cdd:PHA03100 132 ANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIKDVYGFT 194

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119606310 142 ALHYAVYSEILSVVAKLLSHGAVIEVHNKASLTPLLLSITKRSEQIVEFLLIKNANANAVNKY 204
Cdd:PHA03100 195 PLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 64-235 4.61e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 71.92  E-value: 4.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310  64 INLNIQDAQKRTALHWACVNGHEEVVTFLVDRKCQLDVLDGEHRTPLMKALQCHQEACANILIDSGADINLVDVYGNTAL 143
Cdd:PHA02874 115 IDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPL 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310 144 HYAVYSEILSVVAKLLSHGAVIEVHNKASLTPLLLSITkRSEQIVEfLLIKNANANAVNKYKCTALMLAV---ChgSSEI 220
Cdd:PHA02874 195 HNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII-HNRSAIE-LLINNASINDQDIDGSTPLHHAInppC--DIDI 270

                        170
                 ....*....|....*
gi 119606310 221 VGMLLQQNVDVFAAD 235
Cdd:PHA02874 271 IDILLYHKADISIKD 285
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 86-246 1.94e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 69.69  E-value: 1.94e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310  86 EEVVTFLVDRKCQLDVLDGEHRTPLMKALQCHQEACAN-----ILIDSGADINLVDVYGNTALHYAVYSEI--LSVVAKL 158
Cdd:PHA03100  48 IDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLTDVkeivkLLLEYGANVNAPDNNGITPLLYAISKKSnsYSIVEYL 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310 159 LSHGAVIEVHNKASLTPL--LLSITKRSEQIVEFLLIKNANANAVNKYKC----------------TALMLAVCHGSSEI 220
Cdd:PHA03100 128 LDNGANVNIKNSDGENLLhlYLESNKIDLKILKLLIDKGVDINAKNRVNYllsygvpinikdvygfTPLHYAVYNNNPEF 207

                        170       180
                 ....*....|....*....|....*.
gi 119606310 221 VGMLLQQNVDVFAADICGVTAEHYAV 246
Cdd:PHA03100 208 VKYLLDLGANPNLVNKYGDTPLHIAI 233
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 61-245 3.13e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 69.71  E-value: 3.13e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310  61 KKTINLNIQDAQKRTALHWACVNGHEEVVTFLVDRKCQLDV--LDG--------------------EHRT-------PLM 111
Cdd:PHA02876 166 EGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIiaLDDlsvlecavdsknidtikaiiDNRSninkndlSLL 245

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310 112 KALQCHQEACANILIDSGADINLVDVYGNTALHYAVYSEILS-VVAKLLSHGAVIEVHNKASLTPL-LLSITKRSEQIVE 189
Cdd:PHA02876 246 KAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLyLMAKNGYDTENIR 325

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 119606310 190 FLLIKNANANAVNKYKCTALMLA-VCHGSSEIVGMLLQQNVDVFAADICGVTAEHYA 245
Cdd:PHA02876 326 TLIMLGADVNAADRLYITPLHQAsTLDRNKDIVITLLELGANVNARDYCDKTPIHYA 382
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 61-231 1.42e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 67.00  E-value: 1.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310  61 KKTINLNIQDAQKRTALHWACVNGHE-----EVVTFLVDRKCQLDVLDGEHRTPLMKALQCHQEACANI--LIDSGADIN 133
Cdd:PHA03100  56 DNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKKSNSYSIVeyLLDNGANVN 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310 134 LVDVYGNTALHYAVYS-----EILSV-------------VAKLLSHGAVIEVHNKASLTPLLLSITKRSEQIVEFLLIKN 195
Cdd:PHA03100 136 IKNSDGENLLHLYLESnkidlKILKLlidkgvdinaknrVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLG 215

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 119606310 196 ANANAVNKYKCTALMLAVCHGSSEIVGMLLQQNVDV 231
Cdd:PHA03100 216 ANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSI 251
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 74-230 1.08e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 64.24  E-value: 1.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310  74 RTALHWACVNGHEEVVTFLVD-RKCQLDVLDGEHRTPLMKALQCHQEACANILIDSGADINLVDVYGNTALHYAVYSEIL 152
Cdd:PHA02875  69 ESELHDAVEEGDVKAVEELLDlGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI 148

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119606310 153 SVVAKLLSHGAVIEVHNKASLTPLLLSITKRSEQIVEFLLIKNANANAVNKYKCTALM-LAVCHGSSEIVGMLLQQNVD 230
Cdd:PHA02875 149 KGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALcYAIENNKIDIVRLFIKRGAD 227
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 22-260 1.19e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 64.70  E-value: 1.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310  22 SQLVYTSNDSyiVHSGDLRK---IHKAASRGQVRKL-EKMTKRKktINLNIQDAQKRTALHWACVNGHE-EVVTFLVDRK 96
Cdd:PHA02876 256 SLLLYDAGFS--VNSIDDCKntpLHHASQAPSLSRLvPKLLERG--ADVNAKNIKGETPLYLMAKNGYDtENIRTLIMLG 331

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310  97 CQLDVLDGEHRTPLMKALQCHQEACANI-LIDSGADINLVDVYGNTALHYAVYSEILSVVAKLLSHGAVIEVHNKASLTP 175
Cdd:PHA02876 332 ADVNAADRLYITPLHQASTLDRNKDIVItLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTA 411

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310 176 LLLSITKRSEQI-VEFLLIKNANANAVNKYKCTALMLAvCHGSS--EIVGMLLQQNVDVFAADIcgvtAEHYA--VTCGF 250
Cdd:PHA02876 412 LHFALCGTNPYMsVKTLIDRGANVNSKNKDLSTPLHYA-CKKNCklDVIEMLLDNGADVNAINI----QNQYPllIALEY 486

                        250
                 ....*....|
gi 119606310 251 HHIHEQIMEY 260
Cdd:PHA02876 487 HGIVNILLHY 496
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
122-260 2.63e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 61.89  E-value: 2.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310 122 ANILIDSGADINLVDVYGNTALHYAVYSEILSVVAKLLSHGAVIEVHNKASLTPLLLSITKRSEQIVEFLLIKNANANAV 201
Cdd:COG0666    4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 119606310 202 NKYKCTALMLAVCHGSSEIVGMLLQQNVDVFAADICGVTAEHYAVTCGfhhiHEQIMEY 260
Cdd:COG0666   84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNG----NLEIVKL 138
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 49-246 1.28e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 61.13  E-value: 1.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310  49 GQVRKLEKMTKRKKTInLNIQDAQKRTALHWACVNGHEEVVTFLVDRKCQLDVLDGEHRTPLMKALQ------------- 115
Cdd:PHA02874  12 GDIEAIEKIIKNKGNC-INISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKigahdiikllidn 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310 116 ----------CHQEACANILIDSGADINLVDVYGNTALHYAVYSEILSVVAKLLSHGAVIEVHNKASLTPLLLSITKRSE 185
Cdd:PHA02874  91 gvdtsilpipCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFF 170

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119606310 186 QIVEFLLIKNANANAVNKYKCTALMLAVCHGSSEIVGMLLQQNVDVFAADICGVTAEHYAV 246
Cdd:PHA02874 171 DIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI 231
Ank_2 pfam12796
Ankyrin repeats (3 copies);
176-261 2.05e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 54.74  E-value: 2.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310  176 LLLSITKRSEQIVEFLLIKNANANAVNKYKCTALMLAVCHGSSEIVgMLLQQNVDVFAADIcGVTAEHYAVTCGfhhiHE 255
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIV-KLLLEHADVNLKDN-GRTALHYAARSG----HL 74


                  ....*.
gi 119606310  256 QIMEYI 261
Cdd:pfam12796  75 EIVKLL 80
PHA03095 PHA03095
ankyrin-like protein; Provisional
 70-201 2.32e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 60.42  E-value: 2.32e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310  70 DAQKRTALHWACVNGH--EEVVTFLVDRKCQLDVLDGEHRTPL-MKALQChqeACANI----LIDSGADINLVDVYGNTA 142
Cdd:PHA03095 184 DDRFRSLLHHHLQSFKprARIVRELIRAGCDPAATDMLGNTPLhSMATGS---SCKRSlvlpLLIAGISINARNRYGQTP 260

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 119606310 143 LHYAVYSEILSVVAKLLSHGAVIEVHNKASLTPLLLSITKRSEQIVEFLLIKNANANAV 201
Cdd:PHA03095 261 LHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETV 319
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 42-225 3.49e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 59.62  E-value: 3.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310  42 IHKAASRGQVRKLEKMTKRKKTINlNIQDAQKRTALHWACVNGHEEVVTFLVDRKCQLDVLDGEHRTPLMKALQCHQEAC 121
Cdd:PHA02875  72 LHDAVEEGDVKAVEELLDLGKFAD-DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKG 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310 122 ANILIDSGADINLVDVYGNTALHYAVYSEILSVVAKLLSHGAVIE-VHNKASLTPLLLSITKRSEQIVEFLLIKNANANA 200
Cdd:PHA02875 151 IELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDyFGKNGCVAALCYAIENNKIDIVRLFIKRGADCNI 230

                        170       180       190
                 ....*....|....*....|....*....|...
gi 119606310 201 V----NKYkCTALMLaVC----HGSSEIVGMLL 225
Cdd:PHA02875 231 MfmieGEE-CTILDM-ICnmctNLESEAIDALI 261
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 88-314 5.55e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 59.31  E-value: 5.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310  88 VVTFLVDRKCQLDVLDGEHRTPLMKALQCHQEACANILIDSGADINLVDVYGNTALHYAVYSEILSVVAKLLSHGAVIev 167
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNI-- 237

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310 168 hNKASLTpLLLSItkRSEQIVEFLLIKNA--NANAVNKYKCTALMLAVCHGS-SEIVGMLLQQNVDVFAADICGVTAEHY 244
Cdd:PHA02876 238 -NKNDLS-LLKAI--RNEDLETSLLLYDAgfSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYL 313

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119606310 245 AVTCGFHhiheqiMEYIRKLSKNHQNTNPEGTSAGTPDEAAPLAERTPDTAESLVEKTPD-EAAPLVERTP 314
Cdd:PHA02876 314 MAKNGYD------TENIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIVITLLELGANvNARDYCDKTP 378
Ank_4 pfam13637
Ankyrin repeats (many copies);
74-126 2.87e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.35  E-value: 2.87e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 119606310   74 RTALHWACVNGHEEVVTFLVDRKCQLDVLDGEHRTPLMKALQCHQEACANILI 126
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 64-246 7.22e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 55.66  E-value: 7.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310  64 INLNIQDAQKRTALHWACVNGHEEVVTFLVDRKCQLDVLDgehrtplmkALQCHQEACAN--------ILIDSGADINLV 135
Cdd:PHA02878  61 HNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFY---------TLVAIKDAFNNrnveifkiILTNRYKNIQTI 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310 136 DVYGNTALHYAVYSEIlSVVAKLLSHGAVIEVHNKASL-TPLLLSITKRSEQIVEFLLIKNANANAVNKYKCTALMLAVC 214
Cdd:PHA02878 132 DLVYIDKKSKDDIIEA-EITKLLLSYGADINMKDRHKGnTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVK 210

                        170       180       190
                 ....*....|....*....|....*....|..
gi 119606310 215 HGSSEIVGMLLQQNVDVFAADICGVTAEHYAV 246
Cdd:PHA02878 211 HYNKPIVHILLENGASTDARDKCGNTPLHISV 242
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 45-204 8.65e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 55.64  E-value: 8.65e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310  45 AASRGQVRKLEKMTKRKKtiNLNIQDAQKRTALHWACVNGHEEVVTFLVDRKCQLDVLDGEHRTPLMKALQCHQEACANI 124
Cdd:PLN03192 532 VASTGNAALLEELLKAKL--DPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRI 609

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310 125 LIDSGAdinLVDVY-GNTALHYAVYSEILSVVAKLLSHGAVIEVHNKASLTPLLLSITKRSEQIVEFLLIKNANANAVNK 203
Cdd:PLN03192 610 LYHFAS---ISDPHaAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANT 686


                 .
gi 119606310 204 Y 204
Cdd:PLN03192 687 D 687
Ank_2 pfam12796
Ankyrin repeats (3 copies);
209-271 5.19e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 48.19  E-value: 5.19e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119606310  209 LMLAVCHGSSEIVGMLLQQNVDVFAADICGVTAEHYAVTCGFHHIHEQIMEYIRKLSKNHQNT 271
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRT 63
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 72-194 1.78e-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: 51.17  E-value: 1.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310  72 QKRTALHWACVNGHEEVV-----------------TFLVDRKCQLdVLDGEHrtPLMKALQCHQEACANILIDSGADINL 134
Cdd:cd22192   88 QGETALHIAVVNQNLNLVreliargadvvspratgTFFRPGPKNL-IYYGEH--PLSFAACVGNEEIVRLLIEHGADIRA 164

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119606310 135 VDVYGNTALHYAV-----------YSEILSVVAKLLSHgAVIEVHNKASLTPLLLSITKRSEQIVEFLLIK 194
Cdd:cd22192  165 QDSLGNTVLHILVlqpnktfacqmYDLILSYDKEDDLQ-PLDLVPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
Ank_4 pfam13637
Ankyrin repeats (many copies);
42-93 2.75e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.96  E-value: 2.75e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 119606310   42 IHKAASRGQVRKLEkmTKRKKTINLNIQDAQKRTALHWACVNGHEEVVTFLV 93
Cdd:pfam13637   5 LHAAAASGHLELLR--LLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
92-146 4.90e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.26  E-value: 4.90e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 119606310   92 LVDRK-CQLDVLDGEHRTPLMKALQCHQEACANILIDSGADINLVDVYGNTALHYA 146
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 152-273 2.58e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 47.35  E-value: 2.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310 152 LSVVAKLLSHGAVIEVHNKASLTPLLLSITKRSEQIVEFLLIKNANANAVNKYKCTALMLAVCHGSS-----EIVGMLLQ 226
Cdd:PHA03100  15 VKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLE 94

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 119606310 227 QNVDVFAADICGVTAEHYAVTCGFHHIHeqIMEYirkLSKNHQNTNP 273
Cdd:PHA03100  95 YGANVNAPDNNGITPLLYAISKKSNSYS--IVEY---LLDNGANVNI 136
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 45-247 7.04e-05

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: 46.16  E-value: 7.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310  45 AASRGQVRKLEKMTKrKKTINLNIQDAQKRTALHWACVNGHEEVVTFLVDrkcqldvldgehrtplmkalqchqeaCANI 124
Cdd:cd22192   24 AAKENDVQAIKKLLK-CPSCDLFQRGALGETALHVAALYDNLEAAVVLME--------------------------AAPE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310 125 LidsgadINLV---DVY-GNTALHYAVYSEILSVVAKLLSHGAVIevhNKASLTPLLLSITKRS-----EQIVEFllikn 195
Cdd:cd22192   77 L------VNEPmtsDLYqGETALHIAVVNQNLNLVRELIARGADV---VSPRATGTFFRPGPKNliyygEHPLSF----- 142

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 119606310 196 ananavnkykctalmlAVCHGSSEIVGMLLQQNVDVFAADICGVTAEHYAVT 247
Cdd:cd22192  143 ----------------AACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVL 178
Ank_4 pfam13637
Ankyrin repeats (many copies);
139-192 8.06e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.72  E-value: 8.06e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 119606310  139 GNTALHYAVYSEILSVVAKLLSHGAVIEVHNKASLTPLLLSITKRSEQIVEFLL 192
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
173-225 1.17e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.34  E-value: 1.17e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 119606310  173 LTPLLLSITKRSEQIVEFLLIKNANANAVNKYKCTALMLAVCHGSSEIVGMLL 225
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 122-192 1.59e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.89  E-value: 1.59e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119606310 122 ANILIDSGADINLVDVYGNTALHYAVYSEILSVVAKLLSHGAVIEVHNKASLTPLLLSITKRSEQIVEFLL 192
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 119-272 1.90e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 44.57  E-value: 1.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310 119 EACANILIDSGADINLVDVYGNTALHYAVYSEILSVVAKLLSHGAVIEVHNKASLTPLLLSITKRSEQIVEFLLIKNANA 198
Cdd:PHA02874  15 EAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDT 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310 199 -----------------------NAVNKYKCTALMLAVCHGSSEIVGMLLQQNVDVFAADICGVTAEHYAVTCGFHHIHE 255
Cdd:PHA02874  95 silpipciekdmiktildcgidvNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIK 174

                        170
                 ....*....|....*..
gi 119606310 256 QIMEYIRKLSKNHQNTN 272
Cdd:PHA02874 175 LLLEKGAYANVKDNNGE 191
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 108-249 2.60e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 43.83  E-value: 2.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310 108 TPLMKALQCHQEACANILIDSGA--DINLVDVygNTALHYAVYSEILSVVAKLLSHGAVI-EVHNKASLTPLLLSITKRS 184
Cdd:PHA02875  37 SPIKLAMKFRDSEAIKLLMKHGAipDVKYPDI--ESELHDAVEEGDVKAVEELLDLGKFAdDVFYKDGMTPLHLATILKK 114

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119606310 185 EQIVEFLLIKNANANAVNKYKCTALMLAVCHGSSEIVGMLLQQNVDVFAADICGVTAEHYAVTCG 249
Cdd:PHA02875 115 LDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKG 179
PHA02798 PHA02798
ankyrin-like protein; Provisional
 65-231 3.06e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 44.06  E-value: 3.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310  65 NLNIQDAQKRTALHWACVNGH---EEVVTFLVDRKCQLDVLDGEHRTPLMKALQ--CH-QEACANILIDSGADINLV-DV 137
Cdd:PHA02798 101 DINKKNSDGETPLYCLLSNGYinnLEILLFMIENGADTTLLDKDGFTMLQVYLQsnHHiDIEIIKLLLEKGVDINTHnNK 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310 138 YGNTALHYAV---YSEILSVVAKLL-SHGAVIEVHNKAS-------LTPLLLSITKRSEQIVEFLLiKNANANAVNKYKC 206
Cdd:PHA02798 181 EKYDTLHCYFkynIDRIDADILKLFvDNGFIINKENKSHkkkfmeyLNSLLYDNKRFKKNILDFIF-SYIDINQVDELGF 259

                        170       180
                 ....*....|....*....|....*
gi 119606310 207 TALMLAVCHGSSEIVGMLLQQNVDV 231
Cdd:PHA02798 260 NPLYYSVSHNNRKIFEYLLQLGGDI 284
Ank_5 pfam13857
Ankyrin repeats (many copies);
192-245 4.51e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.87  E-value: 4.51e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 119606310  192 LIKN--ANANAVNKYKCTALMLAVCHGSSEIVGMLLQQNVDVFAADICGVTAEHYA 245
Cdd:pfam13857   1 LLEHgpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
64-110 4.93e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.48  E-value: 4.93e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 119606310   64 INLNIQDAQKRTALHWACVNGHEEVVTFLVDRKCQLDVLDGEHRTPL 110
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 72-101 7.28e-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: 7.28e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 119606310    72 QKRTALHWACVNGHEEVVTFLVDRKCQLDV 101
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
207-260 7.59e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.02  E-value: 7.59e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 119606310  207 TALMLAVCHGSSEIVGMLLQQNVDVFAADICGVTAEHYAVTCGfhhiHEQIMEY 260
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNG----NVEVLKL 52
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 74-103 1.46e-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: 36.50  E-value: 1.46e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 119606310   74 RTALHWACV-NGHEEVVTFLVDRKCQLDVLD 103
Cdd:pfam00023   3 NTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 138-170 1.67e-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: 36.50  E-value: 1.67e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 119606310  138 YGNTALHYAVYSE-ILSVVAKLLSHGAVIEVHNK 170
Cdd:pfam00023   1 DGNTPLHLAAGRRgNLEIVKLLLSKGADVNARDK 34
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 72-194 1.71e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 41.79  E-value: 1.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310  72 QKRTALHWACVNGHEEVVTFLVDRKCQLD---------------VLDGEHrtPLMKALQCHQEACANILIDSGADI---N 133
Cdd:cd21882   72 QGQTALHIAIENRNLNLVRLLVENGADVSaratgrffrkspgnlFYFGEL--PLSLAACTNQEEIVRLLLENGAQPaalE 149

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119606310 134 LVDVYGNTALHYAV----------------YSEILSVVAKLLSHGAVIEVHNKASLTPLLLSITKRSEQIVEFLLIK 194
Cdd:cd21882  150 AQDSLGNTVLHALVlqadntpensafvcqmYNLLLSYGAHLDPTQQLEEIPNHQGLTPLKLAAVEGKIVMFQHILQR 226
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 74-101 2.80e-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: 35.70  E-value: 2.80e-03
                          10        20
                  ....*....|....*....|....*...
gi 119606310   74 RTALHWACVNGHEEVVTFLVDRKCQLDV 101
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 67-128 2.90e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.04  E-value: 2.90e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119606310  67 NIQDAQKRTALHWACVNGHEEVVTFLVDRKCQLDVLDGEHRTP---------------LMKALQCHQEACANILIDS 128
Cdd:PTZ00322 109 NCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPlelaeengfrevvqlLSRHSQCHFELGANAKPDS 185
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 206-235 4.84e-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: 35.34  E-value: 4.84e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 119606310  206 CTALMLAVCH-GSSEIVGMLLQQNVDVFAAD 235
Cdd:pfam00023   3 NTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 174-277 5.60e-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: 40.13  E-value: 5.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310 174 TPLLLSITKRSEQIVEFLLIKNANANA---------VNKYKC-----TALMLAVCHGSSEIVGMLLQQ-NVDVFAADICG 238
Cdd:cd22194  143 TALNIAIERRQGDIVKLLIAKGADVNAhakgvffnpKYKHEGfyfgeTPLALAACTNQPEIVQLLMEKeSTDITSQDSRG 222

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 119606310 239 VTAEHYAVTCG--FHHIHEQIMEYIRKLSKNHQNTNPEGTS 277
Cdd:cd22194  223 NTVLHALVTVAedSKTQNDFVKRMYDMILLKSENKNLETIR 263
Ank_5 pfam13857
Ankyrin repeats (many copies);
125-176 7.85e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.01  E-value: 7.85e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 119606310  125 LIDSG-ADINLVDVYGNTALHYAVYSEILSVVAKLLSHGAVIEVHNKASLTPL 176
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 131-251 7.94e-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: 39.68  E-value: 7.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310  131 DINLVDVYGNTAL-HYAVYSEILSVVAKLLSHGAVIEVhNKAsltpLLLSITKRSEQIVE-FLLIKNANAN-------AV 201
Cdd:TIGR00870  44 NINCPDRLGRSALfVAAIENENLELTELLLNLSCRGAV-GDT----LLHAISLEYVDAVEaILLHLLAAFRksgplelAN 118

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 119606310  202 NKYKC------TALMLAVCHGSSEIVGMLLQQNVDVFAADICGVTAEHYAVTCGFH 251
Cdd:TIGR00870 119 DQYTSeftpgiTALHLAAHRQNYEIVKLLLERGASVPARACGDFFVKSQGVDSFYH 174
PHA02791 PHA02791
ankyrin-like protein; Provisional
 128-228 8.32e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 38.87  E-value: 8.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606310 128 SGADINLVDVYGNTALHYAVYSEILSVVAKLLSHGAVIEVHNKAslTPLLLSITKRSEQIVEFLLIKNANANAVNKYKCT 207
Cdd:PHA02791  19 SSKDAFKADVHGHSALYYAIADNNVRLVCTLLNAGALKNLLENE--FPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNT 96

                         90       100
                 ....*....|....*....|.
gi 119606310 208 ALMLAVCHGSSEIVGMLLQQN 228
Cdd:PHA02791  97 ALYYAVDSGNMQTVKLFVKKN 117
 
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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