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Conserved domains on  [gi|1370473440|ref|XP_024306935|]
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ankyrin repeat domain-containing protein 30B isoform X4 [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];
61-272 1.80e-46

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 161.66  E-value: 1.80e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440  61 KKPVNLNKRDMKKRTALHWACVNGHAEVVTFLVDRKCQLNVLDGEGRTPLMKALQCEREACANILIDAGADLNYVDVYGN 140
Cdd:COG0666    75 AAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGN 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440 141 TALHYAVYSENLLMVATLLSYGAVIEVQNKASLTPLLLAIQKRSKQTVEFLLTKNANANAFNESKCTALMLAICEGSSEI 220
Cdd:COG0666   155 TPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI 234

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1370473440 221 VGMLLQQNVDVFAEDIHGITAERYAAACGVNYIHQQLLEHIRKLPKNPQNTN 272
Cdd:COG0666   235 VKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLL 286
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
61-272 1.80e-46

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 161.66  E-value: 1.80e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440  61 KKPVNLNKRDMKKRTALHWACVNGHAEVVTFLVDRKCQLNVLDGEGRTPLMKALQCEREACANILIDAGADLNYVDVYGN 140
Cdd:COG0666    75 AAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGN 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440 141 TALHYAVYSENLLMVATLLSYGAVIEVQNKASLTPLLLAIQKRSKQTVEFLLTKNANANAFNESKCTALMLAICEGSSEI 220
Cdd:COG0666   155 TPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI 234

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1370473440 221 VGMLLQQNVDVFAEDIHGITAERYAAACGVNYIHQQLLEHIRKLPKNPQNTN 272
Cdd:COG0666   235 VKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLL 286
Ank_2 pfam12796
Ankyrin repeats (3 copies);
77-169 7.82e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 83.63  E-value: 7.82e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440  77 LHWACVNGHAEVVTFLVDRKCQLNVLDGEGRTPLMKALQCEREACANILIDaGADLNYVDvYGNTALHYAVYSENLLMVA 156
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1370473440 157 TLLSYGAVIEVQN 169
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 61-203 7.89e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 82.02  E-value: 7.89e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440  61 KKPVNLNKRDMKKRTALHWACVN--GHAEVVTFLVDRKCQLNVLDGEGRTPLMKALQCERE----------------ACA 122
Cdd:PHA03100   94 EYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlkilkllidkgvdinAKN 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440 123 NI--LIDAGADLNYVDVYGNTALHYAVYSENLLMVATLLSYGAVIEVQNKASLTPLLLAIQKRSKQTVEFLLTKNANANA 200
Cdd:PHA03100  174 RVnyLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253


                  ...
gi 1370473440 201 FNE 203
Cdd:PHA03100  254 IIE 256
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 75-194 7.08e-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: 48.09  E-value: 7.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440  75 TALHWACVNGH-----------AEVVT-------FLVDRKCQLNVldgeGRTPLMKALQCEREACANILIDAGADLNYVD 136
Cdd:cd22192    91 TALHIAVVNQNlnlvreliargADVVSpratgtfFRPGPKNLIYY----GEHPLSFAACVGNEEIVRLLIEHGADIRAQD 166

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370473440 137 VYGNTALHYAVYSEN----LLMVATLLSY------GAVIEVQNKASLTPLLLAIQKRSKQTVEFLLTK 194
Cdd:cd22192   167 SLGNTVLHILVLQPNktfaCQMYDLILSYdkeddlQPLDLVPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 45-235 2.83e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 46.23  E-value: 2.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440  45 AASRGQVQKLEKMTVGKKPVNLNKRDMKKRTALHWACV-NGHAEVVTFLVDRKCQLNVldgeGRTPLMKALQCER---EA 120
Cdd:TIGR00870  24 AAERGDLASVYRDLEEPKKLNINCPDRLGRSALFVAAIeNENLELTELLLNLSCRGAV----GDTLLHAISLEYVdavEA 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440 121 CANILIDAGAD-LNYVDVY---------GNTALHYAVYSENLLMVATLLSYGAVIEVQNKAsltplllaiqkrskqtVEF 190
Cdd:TIGR00870 100 ILLHLLAAFRKsGPLELANdqytseftpGITALHLAAHRQNYEIVKLLLERGASVPARACG----------------DFF 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1370473440 191 LLTKNANANAFNESKctaLMLAICEGSSEIVGMLLQQNVDVFAED 235
Cdd:TIGR00870 164 VKSQGVDSFYHGESP---LNAAACLGSPSIVALLSEDPADILTAD 205
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 74-101 2.74e-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: 37.95  E-value: 2.74e-04
                           10        20
                   ....*....|....*....|....*...
gi 1370473440   74 RTALHWACVNGHAEVVTFLVDRKCQLNV 101
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
61-272 1.80e-46

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 161.66  E-value: 1.80e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440  61 KKPVNLNKRDMKKRTALHWACVNGHAEVVTFLVDRKCQLNVLDGEGRTPLMKALQCEREACANILIDAGADLNYVDVYGN 140
Cdd:COG0666    75 AAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGN 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440 141 TALHYAVYSENLLMVATLLSYGAVIEVQNKASLTPLLLAIQKRSKQTVEFLLTKNANANAFNESKCTALMLAICEGSSEI 220
Cdd:COG0666   155 TPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI 234

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1370473440 221 VGMLLQQNVDVFAEDIHGITAERYAAACGVNYIHQQLLEHIRKLPKNPQNTN 272
Cdd:COG0666   235 VKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLL 286
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
64-272 2.20e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 150.87  E-value: 2.20e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440  64 VNLNKRDMKKRTALHWACVNGHAEVVTFLVDRKCQLNVLDGEGRTPLMKALQCEREACANILIDAGADLNYVDVYGNTAL 143
Cdd:COG0666    45 LALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPL 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440 144 HYAVYSENLLMVATLLSYGAVIEVQNKASLTPLLLAIQKRSKQTVEFLLTKNANANAFNESKCTALMLAICEGSSEIVGM 223
Cdd:COG0666   125 HLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKL 204

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1370473440 224 LLQQNVDVFAEDIHGITAERYAAACGVNYIHQQLLEHIRKLPKNPQNTN 272
Cdd:COG0666   205 LLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGL 253
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
42-241 1.25e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 146.25  E-value: 1.25e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440  42 IHTAASRGQVQKLEKMTvgKKPVNLNKRDMKKRTALHWACVNGHAEVVTFLVDRKCQLNVLDGEGRTPLMKALQCEREAC 121
Cdd:COG0666    91 LHAAARNGDLEIVKLLL--EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEI 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440 122 ANILIDAGADLNYVDVYGNTALHYAVYSENLLMVATLLSYGAVIEVQNKASLTPLLLAIQKRSKQTVEFLLTKNANANAF 201
Cdd:COG0666   169 VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAK 248

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1370473440 202 NESKCTALMLAICEGSSEIVGMLLQQNVDVFAEDIHGITA 241
Cdd:COG0666   249 DKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
65-317 2.75e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 121.21  E-value: 2.75e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440  65 NLNKRDMKKRTALHWACVNGHAEVVTFLVDRKCQLNVLDGEGRTPLMKALQCEREACANILIDAGADLNYVDVYGNTALH 144
Cdd:COG0666    13 AALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLH 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440 145 YAVYSENLLMVATLLSYGAVIEVQNKASLTPLLLAIQKRSKQTVEFLLTKNANANAFNESKCTALMLAICEGSSEIVGML 224
Cdd:COG0666    93 AAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440 225 LQQNVDVFAEDIHGITAERYAAACGVNYIHQQLLEHirklPKNPQNTNPEGtstGTPDEAApLAERTPDTAESLLEKTPD 304
Cdd:COG0666   173 LEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA----GADVNAKDNDG---KTALDLA-AENGNLEIVKLLLEAGAD 244

                         250
                  ....*....|...
gi 1370473440 305 EAARLVEGTSAKI 317
Cdd:COG0666   245 LNAKDKDGLTALL 257
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
42-209 3.78e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 118.13  E-value: 3.78e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440  42 IHTAASRGQVQKLEKMTvgKKPVNLNKRDMKKRTALHWACVNGHAEVVTFLVDRKCQLNVLDGEGRTPLMKALQCEREAC 121
Cdd:COG0666   124 LHLAAYNGNLEIVKLLL--EAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEI 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440 122 ANILIDAGADLNYVDVYGNTALHYAVYSENLLMVATLLSYGAVIEVQNKASLTPLLLAIQKRSKQTVEFLLTKNANANAF 201
Cdd:COG0666   202 VKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAA 281


                  ....*...
gi 1370473440 202 NESKCTAL 209
Cdd:COG0666   282 LLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
77-169 7.82e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 83.63  E-value: 7.82e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440  77 LHWACVNGHAEVVTFLVDRKCQLNVLDGEGRTPLMKALQCEREACANILIDaGADLNYVDvYGNTALHYAVYSENLLMVA 156
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1370473440 157 TLLSYGAVIEVQN 169
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
42-136 7.28e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.15  E-value: 7.28e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440  42 IHTAASRGQVQKLEKMTvgKKPVNLNKRDMKKRTALHWACVNGHAEVVTFLVDrKCQLNVLDgEGRTPLMKALQCEREAC 121
Cdd:pfam12796   1 LHLAAKNGNLELVKLLL--ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEI 76

                          90
                  ....*....|....*
gi 1370473440 122 ANILIDAGADLNYVD 136
Cdd:pfam12796  77 VKLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 61-203 7.89e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 82.02  E-value: 7.89e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440  61 KKPVNLNKRDMKKRTALHWACVN--GHAEVVTFLVDRKCQLNVLDGEGRTPLMKALQCERE----------------ACA 122
Cdd:PHA03100   94 EYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlkilkllidkgvdinAKN 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440 123 NI--LIDAGADLNYVDVYGNTALHYAVYSENLLMVATLLSYGAVIEVQNKASLTPLLLAIQKRSKQTVEFLLTKNANANA 200
Cdd:PHA03100  174 RVnyLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253


                  ...
gi 1370473440 201 FNE 203
Cdd:PHA03100  254 IIE 256
Ank_2 pfam12796
Ankyrin repeats (3 copies);
143-235 1.67e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.38  E-value: 1.67e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440 143 LHYAVYSENLLMVATLLSYGAVIEVQNKASLTPLLLAIQKRSKQTVEFLLtKNANANAFNESKcTALMLAICEGSSEIVG 222
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDNGR-TALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1370473440 223 MLLQQNVDVFAED 235
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 64-213 2.18e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 77.61  E-value: 2.18e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440  64 VNLNKRDmKKRTALHWACVNGHAEVVTFLVDRKCQLNVLDGEGRTPLMKALQCEREACANILIDAGADLNYVDVYGNTAL 143
Cdd:PHA02878  160 INMKDRH-KGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPL 238

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370473440 144 HYAV-YSENLLMVATLLSYGAVIEVQNKA-SLTPLLLAIqkRSKQTVEFLLTKNANANAFNESKCTALMLAI 213
Cdd:PHA02878  239 HISVgYCKDYDILKLLLEHGVDVNAKSYIlGLTALHSSI--KSERKLKLLLEYGADINSLNSYKLTPLSSAV 308
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 64-238 5.97e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 76.16  E-value: 5.97e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440  64 VNLNKRDMKKRTALHWACVNGHAEVVTFLVDRKCQLNVLDGEGRTPLMKALQCEREACANILIDAGADLNYVDVYGNTAL 143
Cdd:PHA02874  115 IDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPL 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440 144 HYAVYSENLLMVATLLSYGAVIEVQNKASLTPLLLAIQkRSKQTVEfLLTKNANANAFNESKCTALMLAI---CegSSEI 220
Cdd:PHA02874  195 HNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII-HNRSAIE-LLINNASINDQDIDGSTPLHHAInppC--DIDI 270

                         170
                  ....*....|....*...
gi 1370473440 221 VGMLLQQNVDVFAEDIHG 238
Cdd:PHA02874  271 IDILLYHKADISIKDNKG 288
PHA03095 PHA03095
ankyrin-like protein; Provisional
 86-241 2.49e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 74.29  E-value: 2.49e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440  86 AEVVTFLVDRKCQLNVLDGEGRTPLMKALQCEREACANI---LIDAGADLNYVDVYGNTALHYAVYSENLL-MVATLLSY 161
Cdd:PHA03095   27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKA 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440 162 GAVIEVQNKASLTPL--LLAIQKRSKQTVEFLLTKNANANAFNESKCTAlmLAICEGSS----EIVGMLLQQNVDVFAED 235
Cdd:PHA03095  107 GADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTP--LAVLLKSRnanvELLRLLIDAGADVYAVD 184


                  ....*.
gi 1370473440 236 IHGITA 241
Cdd:PHA03095  185 DRFRSL 190
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 61-236 2.88e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 74.71  E-value: 2.88e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440  61 KKPVNLNKRDMKKRTALHWACVNGH-AEVVTFLVDRKCQLNVLDGEGRTPLMKALQCEREACANI-LIDAGADLNYVDVY 138
Cdd:PHA02876  295 ERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIVItLLELGANVNARDYC 374

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440 139 GNTALHYAVYSENLLMVATLLSYGAVIEVQNKASLTPLLLAIQKRSKQT-VEFLLTKNANANAFNESKCTALMLAiCEGS 217
Cdd:PHA02876  375 DKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVNSKNKDLSTPLHYA-CKKN 453

                         170       180
                  ....*....|....*....|.
gi 1370473440 218 S--EIVGMLLQQNVDVFAEDI 236
Cdd:PHA02876  454 CklDVIEMLLDNGADVNAINI 474
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 61-260 9.96e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 70.09  E-value: 9.96e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440  61 KKPVNLNKRDMKKRTALHWACVNGHAEVVTFLVDRKCQLNVLDGEGRT-----------------------------PLM 111
Cdd:PHA02876  166 EGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSvlecavdsknidtikaiidnrsninkndlSLL 245

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440 112 KALQCEREACANILIDAGADLNYVDVYGNTALHYAVYSENL-LMVATLLSYGAVIEVQNKASLTPL-LLAIQKRSKQTVE 189
Cdd:PHA02876  246 KAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLyLMAKNGYDTENIR 325

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370473440 190 FLLTKNANANAFNESKCTALMLA-ICEGSSEIVGMLLQQNVDVFAEDIHGITAERYAAACGVNYIHQQLLEH 260
Cdd:PHA02876  326 TLIMLGADVNAADRLYITPLHQAsTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDY 397
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 57-230 1.56e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 68.86  E-value: 1.56e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440  57 MTVGKKPvNLNKRDMkkRTALHWACVNGHAEVVTFLVDRKCQLN-VLDGEGRTPLMKALQCEREACANILIDAGADLNYV 135
Cdd:PHA02875   55 MKHGAIP-DVKYPDI--ESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIP 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440 136 DVYGNTALHYAVYSENLLMVATLLSYGAVIEVQNKASLTPLLLAIQKRSKQTVEFLLTKNANANAFNESKCTALM-LAIC 214
Cdd:PHA02875  132 NTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALcYAIE 211

                         170
                  ....*....|....*.
gi 1370473440 215 EGSSEIVGMLLQQNVD 230
Cdd:PHA02875  212 NNKIDIVRLFIKRGAD 227
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 61-231 2.76e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 67.77  E-value: 2.76e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440  61 KKPVNLNKRDMKKRTALHWACVNGHA-----EVVTFLVDRKCQLNVLDGEGRTPLMKALQCEREACANI--LIDAGADLN 133
Cdd:PHA03100   56 DNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKKSNSYSIVeyLLDNGANVN 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440 134 YVDVYGNTALHYAVYS--------ENLL----------MVATLLSYGAVIEVQNKASLTPLLLAIQKRSKQTVEFLLTKN 195
Cdd:PHA03100  136 IKNSDGENLLHLYLESnkidlkilKLLIdkgvdinaknRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLG 215

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1370473440 196 ANANAFNESKCTALMLAICEGSSEIVGMLLQQNVDV 231
Cdd:PHA03100  216 ANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSI 251
PHA03095 PHA03095
ankyrin-like protein; Provisional
 61-310 5.17e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 67.36  E-value: 5.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440  61 KKPVNLNKRDMKKRTALHwACVNG---HAEVVTFLVDRKCQLNVLDGEGRTPLmKALQCEREACA---NILIDAGADLNY 134
Cdd:PHA03095  105 KAGADVNAKDKVGRTPLH-VYLSGfniNPKVIRLLLRKGADVNALDLYGMTPL-AVLLKSRNANVellRLLIDAGADVYA 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440 135 VDVYGNTALHY-AVYS-ENLLMVATLLSYGAVIEVQNKASLTPL-LLAIQKRSKQT-VEFLLTKNANANAFNESKCTALM 210
Cdd:PHA03095  183 VDDRFRSLLHHhLQSFkPRARIVRELIRAGCDPAATDMLGNTPLhSMATGSSCKRSlVLPLLIAGISINARNRYGQTPLH 262

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440 211 LAICEGSSEIVGMLLQQNVDVFAEDIHGITaeryaaaCGVNYIHQqllEHIRK----LPKNPqntnpegtstgtpdeAAP 286
Cdd:PHA03095  263 YAAVFNNPRACRRLIALGADINAVSSDGNT-------PLSLMVRN---NNGRAvraaLAKNP---------------SAE 317

                         250       260
                  ....*....|....*....|....
gi 1370473440 287 LAERTPDTAESLLEKTPDEAARLV 310
Cdd:PHA03095  318 TVAATLNTASVAGGDIPSDATRLC 341
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 123-235 1.07e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 66.23  E-value: 1.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440 123 NILIDAGADLNYVDVYGNTALHY-----AVYSENLLMVATLLSYGAVIEVQNKASLTPLLLAIQKRSKQT--VEFLLTKN 195
Cdd:PHA03100   52 KILLDNGADINSSTKNNSTPLHYlsnikYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKKSNSYsiVEYLLDNG 131

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1370473440 196 ANANAFNESKCTALMLAI--CEGSSEIVGMLLQQNVDVFAED 235
Cdd:PHA03100  132 ANVNIKNSDGENLLHLYLesNKIDLKILKLLIDKGVDINAKN 173
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 122-308 1.72e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 66.24  E-value: 1.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440 122 ANILIDAGADLNYVDVYGNTALHYAVYSENLLMVATLLSYGAVIEVQNKASLTPLLLAIQKRSKQTVEFLLTKNANANA- 200
Cdd:PHA02876  161 AEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKn 240

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440 201 --------FNESKCTALML----------AICEGS-----------SEIVGMLLQQNVDVFAEDIHGITAERYAAACGVN 251
Cdd:PHA02876  241 dlsllkaiRNEDLETSLLLydagfsvnsiDDCKNTplhhasqapslSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYD 320

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1370473440 252 yihqqlLEHIRKLPKNPQNTNPEGTSTGTPDEAAPLAERTPDTAESLLEKTPDEAAR 308
Cdd:PHA02876  321 ------TENIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIVITLLELGANVNAR 371
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 107-234 3.09e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.55  E-value: 3.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440 107 RTPLMKALQCEREACANILIDAGADLNyvDVY---GNTALHYAVYSENLLMVATLLSYGAVIEVQNKASLTPLLLAIQKR 183
Cdd:PHA02875   69 ESELHDAVEEGDVKAVEELLDLGKFAD--DVFykdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMG 146

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1370473440 184 SKQTVEFLLTKNANANAFNESKCTALMLAICEGSSEIVGMLLQQ--NVDVFAE 234
Cdd:PHA02875  147 DIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSgaNIDYFGK 199
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
122-315 9.63e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 59.20  E-value: 9.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440 122 ANILIDAGADLNYVDVYGNTALHYAVYSENLLMVATLLSYGAVIEVQNKASLTPLLLAIQKRSKQTVEFLLTKNANANAF 201
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440 202 NESKCTALMLAICEGSSEIVGMLLQQNVDVFAEDIHGITAERYAAACGVNYIHQQLLEHirklPKNPQNTNPEGTstgTP 281
Cdd:COG0666    84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA----GADVNAQDNDGN---TP 156

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1370473440 282 -DEAAplAERTPDTAESLLEKTPDEAARLVEGTSA 315
Cdd:COG0666   157 lHLAA--ANGNLEIVKLLLEAGADVNARDNDGETP 189
Ank_4 pfam13637
Ankyrin repeats (many copies);
74-126 5.87e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.89  E-value: 5.87e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1370473440  74 RTALHWACVNGHAEVVTFLVDRKCQLNVLDGEGRTPLMKALQCEREACANILI 126
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 87-245 1.00e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 56.90  E-value: 1.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440  87 EVVTFLVDRKCQLNVLDGEGRTPLMKALQCEREACANILIDAGADLNYVDVYGNTALHYAVYSENLLMVATLLSYGAVIE 166
Cdd:PHA02874  105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370473440 167 VQNKASLTPLLLAIQKRSKQTVEFLLTKNANANAFNESKCTALMLAICEGSSEIvgMLLQQNVDVFAEDIHGITAERYA 245
Cdd:PHA02874  185 VKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAI--ELLINNASINDQDIDGSTPLHHA 261
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 44-202 2.44e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 56.03  E-value: 2.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440  44 TAASRGQVQKLEKMTVGKKPVNLNkrDMKKRTALHWACVNGHAEVVTFLVDRKCQLNVLDGEGRTPLMKALQCEREACAN 123
Cdd:PLN03192  531 TVASTGNAALLEELLKAKLDPDIG--DSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFR 608

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440 124 ILID--------AGADLnyvdvygntaLHYAVYSENLLMVATLLSYGAVIEVQNKASLTPLLLAIQKRSKQTVEFLLTKN 195
Cdd:PLN03192  609 ILYHfasisdphAAGDL----------LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNG 678


                  ....*..
gi 1370473440 196 ANANAFN 202
Cdd:PLN03192  679 ADVDKAN 685
Ank_4 pfam13637
Ankyrin repeats (many copies);
106-159 4.87e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.20  E-value: 4.87e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1370473440 106 GRTPLMKALQCEREACANILIDAGADLNYVDVYGNTALHYAVYSENLLMVATLL 159
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 75-240 5.07e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 54.58  E-value: 5.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440  75 TALHWACVNGHAEVVTFLVDRKCQLNVLDGEGRTPLMKALQ-----------------------CEREACANILIDAGAD 131
Cdd:PHA02874   37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKigahdiikllidngvdtsilpipCIEKDMIKTILDCGID 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440 132 LNYVDVYGNTALHYAVYSENLLMVATLLSYGAVIEVQNKASLTPLLLAIQKRSKQTVEFLLTKNANANAFNESKCTALML 211
Cdd:PHA02874  117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196

                         170       180
                  ....*....|....*....|....*....
gi 1370473440 212 AICEGSSEIVGMLLQQNVDVFAEDIHGIT 240
Cdd:PHA02874  197 AAEYGDYACIKLLIDHGNHIMNKCKNGFT 225
Ank_4 pfam13637
Ankyrin repeats (many copies);
139-192 6.41e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.81  E-value: 6.41e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1370473440 139 GNTALHYAVYSENLLMVATLLSYGAVIEVQNKASLTPLLLAIQKRSKQTVEFLL 192
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
63-110 9.02e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.50  E-value: 9.02e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1370473440  63 PVNLNKRDMKKRTALHWACVNGHAEVVTFLVDRKCQLNVLDGEGRTPL 110
Cdd:pfam13857   6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 74-259 1.29e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 53.46  E-value: 1.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440  74 RTALHWACVNGHAEVVTFLVDRKCQLNVLDGEGRTPLMKALQCEREACANILIDAGA--DLNYVDVygNTALHYAVYSEN 151
Cdd:PHA02875    3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAipDVKYPDI--ESELHDAVEEGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440 152 LLMVATLLSYGAVI-EVQNKASLTPLLLAIQKRSKQTVEFLLTKNANANAFNESKCTALMLAICEGSSEIVGMLLQQNVD 230
Cdd:PHA02875   81 VKAVEELLDLGKFAdDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKAC 160

                         170       180
                  ....*....|....*....|....*....
gi 1370473440 231 VFAEDIHGITAERYAAACGVNYIHQQLLE 259
Cdd:PHA02875  161 LDIEDCCGCTPLIIAMAKGDIAICKMLLD 189
Ank_5 pfam13857
Ankyrin repeats (many copies);
92-146 5.58e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.19  E-value: 5.58e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370473440  92 LVDRK-CQLNVLDGEGRTPLMKALQCEREACANILIDAGADLNYVDVYGNTALHYA 146
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 75-194 7.08e-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: 48.09  E-value: 7.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440  75 TALHWACVNGH-----------AEVVT-------FLVDRKCQLNVldgeGRTPLMKALQCEREACANILIDAGADLNYVD 136
Cdd:cd22192    91 TALHIAVVNQNlnlvreliargADVVSpratgtfFRPGPKNLIYY----GEHPLSFAACVGNEEIVRLLIEHGADIRAQD 166

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370473440 137 VYGNTALHYAVYSEN----LLMVATLLSY------GAVIEVQNKASLTPLLLAIQKRSKQTVEFLLTK 194
Cdd:cd22192   167 SLGNTVLHILVLQPNktfaCQMYDLILSYdkeddlQPLDLVPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 131-249 7.92e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 47.74  E-value: 7.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440 131 DLNYVDVYGNTA-LHYAVYSENLLMVATLLSYGAVIEVQNKASLTPLLL-----AIQKRSKQTVEFLLTKNANANAFNES 204
Cdd:PHA03100   26 DLNDYSYKKPVLpLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYlsnikYNLTDVKEIVKLLLEYGANVNAPDNN 105

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1370473440 205 KCTALMLAICE--GSSEIVGMLLQQNVDVFAEDIHGITAERYAAACG 249
Cdd:PHA03100  106 GITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESN 152
Ank_5 pfam13857
Ankyrin repeats (many copies);
125-179 1.23e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 1.23e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370473440 125 LIDAG-ADLNYVDVYGNTALHYAVYSENLLMVATLLSYGAVIEVQNKASLTPLLLA 179
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 43-125 1.77e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.82  E-value: 1.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440  43 HTAASRGQVQKLEKMTVGKKPvnlNKRDMKKRTALHWACVNGHAEVVTFLVDRKCQLNVLDGEGRTPLMKALQCEREACA 122
Cdd:PTZ00322   88 QLAASGDAVGARILLTGGADP---NCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVV 164


                  ...
gi 1370473440 123 NIL 125
Cdd:PTZ00322  165 QLL 167
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 64-260 1.77e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 46.80  E-value: 1.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440  64 VNLNKRDMKKRTALHWACVNGHAEVVTFLVDRKCQLNVLDgegrtplmkALQCEREACAN--------ILIDAGADLNYV 135
Cdd:PHA02878   61 HNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFY---------TLVAIKDAFNNrnveifkiILTNRYKNIQTI 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440 136 DVYGNTALHYAVYSENLLmVATLLSYGAVIEVQNKASL-TPLLLAIQKRSKQTVEFLLTKNANANAFNESKCTALMLAIC 214
Cdd:PHA02878  132 DLVYIDKKSKDDIIEAEI-TKLLLSYGADINMKDRHKGnTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVK 210

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1370473440 215 EGSSEIVGMLLQQNVDVFAEDIHGITAERYAAACGVNY-IHQQLLEH 260
Cdd:PHA02878  211 HYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDYdILKLLLEH 257
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 122-192 2.55e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.43  E-value: 2.55e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370473440 122 ANILIDAGADLNYVDVYGNTALHYAVYSENLLMVATLLSYGAVIEVQNKASLTPLLLAIQKRSKQTVEFLL 192
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 45-240 2.78e-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: 2.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440  45 AASRGQVQKLEKMtVGKKPVNLNKRDMKKRTALHWACVNGHAEVVTFLVDrkcqlnvldgegrtplmkalqcereaCANI 124
Cdd:cd22192    24 AAKENDVQAIKKL-LKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--------------------------AAPE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440 125 LIDAGADlnyVDVY-GNTALHYAVYSENLLMVATLLSYGAviEVQNkasltplllaiqkrSKQTVEFLLTKNANANAFNE 203
Cdd:cd22192    77 LVNEPMT---SDLYqGETALHIAVVNQNLNLVRELIARGA--DVVS--------------PRATGTFFRPGPKNLIYYGE 137

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1370473440 204 SkctALMLAICEGSSEIVGMLLQQNVDVFAEDIHGIT 240
Cdd:cd22192   138 H---PLSFAACVGNEEIVRLLIEHGADIRAQDSLGNT 171
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 45-235 2.83e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 46.23  E-value: 2.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440  45 AASRGQVQKLEKMTVGKKPVNLNKRDMKKRTALHWACV-NGHAEVVTFLVDRKCQLNVldgeGRTPLMKALQCER---EA 120
Cdd:TIGR00870  24 AAERGDLASVYRDLEEPKKLNINCPDRLGRSALFVAAIeNENLELTELLLNLSCRGAV----GDTLLHAISLEYVdavEA 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440 121 CANILIDAGAD-LNYVDVY---------GNTALHYAVYSENLLMVATLLSYGAVIEVQNKAsltplllaiqkrskqtVEF 190
Cdd:TIGR00870 100 ILLHLLAAFRKsGPLELANdqytseftpGITALHLAAHRQNYEIVKLLLERGASVPARACG----------------DFF 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1370473440 191 LLTKNANANAFNESKctaLMLAICEGSSEIVGMLLQQNVDVFAED 235
Cdd:TIGR00870 164 VKSQGVDSFYHGESP---LNAAACLGSPSIVALLSEDPADILTAD 205
PHA02791 PHA02791
ankyrin-like protein; Provisional
 136-228 5.64e-05

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 44.65  E-value: 5.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440 136 DVYGNTALHYAVYSENLLMVATLLSYGAVIEVQNKAslTPLLLAIQKRSKQTVEFLLTKNANANAFNESKCTALMLAICE 215
Cdd:PHA02791   27 DVHGHSALYYAIADNNVRLVCTLLNAGALKNLLENE--FPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDS 104

                          90
                  ....*....|...
gi 1370473440 216 GSSEIVGMLLQQN 228
Cdd:PHA02791  105 GNMQTVKLFVKKN 117
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 99-249 5.69e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 44.95  E-value: 5.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440  99 LNVLDGEGRTPLMKALQCEREACANILIDAGADLNYVDVYGNTALHYA--VYSENLL---------------------MV 155
Cdd:PHA02874   28 INISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAikIGAHDIIkllidngvdtsilpipciekdMI 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440 156 ATLLSYGAVIEVQNKASLTPLLLAIQKRSKQTVEFLLTKNANANAFNESKCTALMLAICEGSSEIVGMLLQQNVDVFAED 235
Cdd:PHA02874  108 KTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKD 187

                         170
                  ....*....|....
gi 1370473440 236 IHGITAERYAAACG 249
Cdd:PHA02874  188 NNGESPLHNAAEYG 201
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 138-170 1.17e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.19  E-value: 1.17e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1370473440 138 YGNTALHYAVYSENLL-MVATLLSYGAVIEVQNK 170
Cdd:pfam00023   1 DGNTPLHLAAGRRGNLeIVKLLLSKGADVNARDK 34
Ank_4 pfam13637
Ankyrin repeats (many copies);
42-93 1.29e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.57  E-value: 1.29e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1370473440  42 IHTAASRGQVQKLEKMTvgKKPVNLNKRDMKKRTALHWACVNGHAEVVTFLV 93
Cdd:pfam13637   5 LHAAAASGHLELLRLLL--EKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02791 PHA02791
ankyrin-like protein; Provisional
 38-155 1.37e-04

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 43.49  E-value: 1.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440  38 DLGKIHTAASRgqvqKLEKMTVGKKPVnlnKRDMKKRTALHWACVNGHAEVVTFLVDRKCQLNVLDGEgrTPLMKALQCE 117
Cdd:PHA02791    2 DLSRINTWKSK----QLKSFLSSKDAF---KADVHGHSALYYAIADNNVRLVCTLLNAGALKNLLENE--FPLHQAATLE 72

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1370473440 118 REACANILIDAGADLNYVDVYGNTALHYAVYSENLLMV 155
Cdd:PHA02791   73 DTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGNMQTV 110
Ank_2 pfam12796
Ankyrin repeats (3 copies);
209-271 1.88e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 40.10  E-value: 1.88e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370473440 209 LMLAICEGSSEIVGMLLQQNVDVFAEDIHGITAERYAAACGVNYIHQQLLEHIRKLPKNPQNT 271
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRT 63
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 108-179 2.36e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 42.66  E-value: 2.36e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370473440 108 TPLMKALQCEREACANILIDAGADLN-YVDVYGNTALHYAVYSENLLMVATLLSYGAVIEVQNKASLTPLLLA 179
Cdd:PHA02884   72 NPLIYAIDCDNDDAAKLLIRYGADVNrYAEEAKITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELA 144
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 74-101 2.74e-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: 37.95  E-value: 2.74e-04
                           10        20
                   ....*....|....*....|....*...
gi 1370473440   74 RTALHWACVNGHAEVVTFLVDRKCQLNV 101
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 106-240 2.77e-04

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: 43.33  E-value: 2.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440 106 GRTPLMKA---LQCEREACANILIDAGADLN---------YVDVY--GNTALHYAVYSENLLMVATLLSYGAVIEVQnka 171
Cdd:cd21882    26 GKTCLHKAalnLNDGVNEAIMLLLEAAPDSGnpkelvnapCTDEFyqGQTALHIAIENRNLNLVRLLVENGADVSAR--- 102

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370473440 172 sltplllaiqkrskqtveflltknANANAFNESKCTA-------LMLAICEGSSEIVGMLLQ---QNVDVFAEDIHGIT 240
Cdd:cd21882   103 ------------------------ATGRFFRKSPGNLfyfgelpLSLAACTNQEEIVRLLLEngaQPAALEAQDSLGNT 157
Ank_4 pfam13637
Ankyrin repeats (many copies);
173-225 3.81e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.02  E-value: 3.81e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1370473440 173 LTPLLLAIQKRSKQTVEFLLTKNANANAFNESKCTALMLAICEGSSEIVGMLL 225
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 61-138 4.58e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 42.34  E-value: 4.58e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370473440  61 KKPVNLNKRDMKKRTALHWACVNGHAEVVTFLVDRKCQLNVLDGEGRTPLMKALQCEREACANILIDAGADLNYVDVY 138
Cdd:PHA03100  180 SYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 138-167 4.62e-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: 4.62e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1370473440  138 YGNTALHYAVYSENLLMVATLLSYGAVIEV 167
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 74-103 6.21e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.88  E-value: 6.21e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1370473440  74 RTALHWACV-NGHAEVVTFLVDRKCQLNVLD 103
Cdd:pfam00023   3 NTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 74-101 8.85e-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: 8.85e-04
                          10        20
                  ....*....|....*....|....*...
gi 1370473440  74 RTALHWACVNGHAEVVTFLVDRKCQLNV 101
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 42-243 1.19e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 41.20  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440  42 IHTAASRGQVQKLEKMtVGKKPVNLNKRDMKKRTALHWACV--NGHAEVVTFLVDrkCQLnVLDGEGRTPLMKALQCErE 119
Cdd:PHA02876   45 IHQALQLRQIDIVEEI-IQQNPELIYITDHKCHSTLHTICIipNVMDIVISLTLD--CDI-ILDIKYASIILNKHKLD-E 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440 120 ACANILIDA--GADLNYVDVygNTALHYA------VYSENLLMVATLLSYGAVIEVQNKASLTPLLLAIQKRSKQTVEFL 191
Cdd:PHA02876  120 ACIHILKEAisGNDIHYDKI--NESIEYMklikerIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLL 197

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1370473440 192 LTKNANANAFNESKCTALMLAICEGSSEIVGMLLQQNVDVFAEDIHGITAER 243
Cdd:PHA02876  198 LSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNDLSLLKAIR 249
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 84-247 2.13e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 40.24  E-value: 2.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440  84 GHAEVVTFLVDRKCQLNVLDGEGRTPLMKALQCEREACANILIDAGADLNYVDVYGNTALHYAVYSENLLMVATLLSYGA 163
Cdd:PLN03192  536 GNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFAS 615

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440 164 VievqnkasltplllaiqkrskqtveflltknANANAFNESKCTALMlaicEGSSEIVGMLLQQNVDVFAEDIHGITAER 243
Cdd:PLN03192  616 I-------------------------------SDPHAAGDLLCTAAK----RNDLTAMKELLKQGLNVDSEDHQGATALQ 660


                  ....
gi 1370473440 244 YAAA 247
Cdd:PLN03192  661 VAMA 664
Ank_5 pfam13857
Ankyrin repeats (many copies);
195-245 2.49e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.79  E-value: 2.49e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1370473440 195 NANANAFNESKCTALMLAICEGSSEIVGMLLQQNVDVFAEDIHGITAERYA 245
Cdd:pfam13857   6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 147-230 2.52e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 39.95  E-value: 2.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440 147 VYSENLLMVATLL-SYGAVIEVQNKASLTPLLLAIQKRSKQTVEFLLTKNANANAFNESKCTALMLAICEGSSEIVGMLL 225
Cdd:PHA02874    9 IYSGDIEAIEKIIkNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI 88


                  ....*
gi 1370473440 226 QQNVD 230
Cdd:PHA02874   89 DNGVD 93
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 58-132 2.90e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 40.05  E-value: 2.90e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370473440  58 TVGKKPVNLNKRDMKKRTALHWACVNG-HAEVVTFLVDRKCQLNVLDGEGRTPLMKALqcEREACANILIDAGADL 132
Cdd:PHA02876  427 TLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLHYGAEL 500
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 105-134 3.71e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.87  E-value: 3.71e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1370473440  105 EGRTPLMKALQCEREACANILIDAGADLNY 134
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02798 PHA02798
ankyrin-like protein; Provisional
 61-199 4.25e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 39.43  E-value: 4.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440  61 KKPVNLNKRDMK-KRTALH------WACVNghAEVVTFLVDRKCQLNVLDGEGRTPLMKALQC----EREACANIL--ID 127
Cdd:PHA02798  169 EKGVDINTHNNKeKYDTLHcyfkynIDRID--ADILKLFVDNGFIINKENKSHKKKFMEYLNSllydNKRFKKNILdfIF 246

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370473440 128 AGADLNYVDVYGNTALHYAVYSENLLMVATLLSYGAVIEVQNKASLTPLLLAIQKRSKQTVEFLLTKNANAN 199
Cdd:PHA02798  247 SYIDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNKKPNKN 318
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 105-136 4.85e-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: 34.57  E-value: 4.85e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1370473440 105 EGRTPLMKA-LQCEREACANILIDAGADLNYVD 136
Cdd:pfam00023   1 DGNTPLHLAaGRRGNLEIVKLLLSKGADVNARD 33
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 68-196 8.21e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 36.78  E-value: 8.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440  68 KRDMKKRTALHWACVNGhaEVVTFLVDRkcqlNVLDGEGRTPLMK----ALQC-----------EREACaNILIDAGADL 132
Cdd:PHA02736   12 EPDIEGENILHYLCRNG--GVTDLLAFK----NAISDENRYLVLEynrhGKQCvhivsnpdkadPQEKL-KLLMEWGADI 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370473440 133 NYVD-VYGNTALHYAVYSENlLMVATLLSY--GAVIEVQNKASLTPLLLAIQKRSKQTVEFLLTKNA 196
Cdd:PHA02736   85 NGKErVFGNTPLHIAVYTQN-YELATWLCNqpGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGA 150
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 72-179 8.25e-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: 38.32  E-value: 8.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440  72 KKRTALHWACVNGHAEVVTFLVDRKCQLNV-LDGE------------GRTPLMKALQCEREACANILIDAGAD---LNYV 135
Cdd:cd21882    72 QGQTALHIAIENRNLNLVRLLVENGADVSArATGRffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQpaaLEAQ 151

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440 136 DVYGNTALHYAVYSEN---------LLMVATLLSYGA-------VIEVQNKASLTPLLLA 179
Cdd:cd21882   152 DSLGNTVLHALVLQADntpensafvCQMYNLLLSYGAhldptqqLEEIPNHQGLTPLKLA 211
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 106-240 8.70e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 38.24  E-value: 8.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473440 106 GRTPLMKA---LQCEREACANILIDAGADLN---------YVDVY--GNTALHYAVYSENLLMVATLLSYGAVIEVQNKA 171
Cdd:cd22193    29 GKTCLMKAllnLNPGTNDTIRILLDIAEKTDnlkrfinaeYTDEYyeGQTALHIAIERRQGDIVALLVENGADVHAHAKG 108

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370473440 172 SLtplllaiqkrskqtveFLLTKNANANAFNEskcTALMLAICEGSSEIVGMLLQ---QNVDVFAEDIHGIT 240
Cdd:cd22193   109 RF----------------FQPKYQGEGFYFGE---LPLSLAACTNQPDIVQYLLEnehQPADIEAQDSRGNT 161
 
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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