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Conserved domains on  [gi|2024369857|ref|XP_040544545|]
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ankyrin repeat domain-containing protein 29 isoform X3 [Gallus gallus]

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];
16-239 1.57e-41

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 144.33  E-value: 1.57e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857  16 LANAAFWAARKGNLALLQLLLNSGRVDVDCKDSSGATALFFAAQQGHNDVVKFLFEFGASTEFKNKDGGTALLAACQYGH 95
Cdd:COG0666    53 LGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGN 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857  96 TKVVETLLKHGANVHDQLYDGASAIFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGAER 175
Cdd:COG0666   133 LEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADV 212

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024369857 176 DAARDDGTTALLKAAIKGYNNVIEELLKF-SPTLGLLKNGTSALHAAVLSGNVRTVALLLEAGAD 239
Cdd:COG0666   213 NAKDNDGKTALDLAAENGNLEIVKLLLEAgADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLL 277
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
16-239 1.57e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 144.33  E-value: 1.57e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857  16 LANAAFWAARKGNLALLQLLLNSGRVDVDCKDSSGATALFFAAQQGHNDVVKFLFEFGASTEFKNKDGGTALLAACQYGH 95
Cdd:COG0666    53 LGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGN 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857  96 TKVVETLLKHGANVHDQLYDGASAIFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGAER 175
Cdd:COG0666   133 LEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADV 212

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024369857 176 DAARDDGTTALLKAAIKGYNNVIEELLKF-SPTLGLLKNGTSALHAAVLSGNVRTVALLLEAGAD 239
Cdd:COG0666   213 NAKDNDGKTALDLAAENGNLEIVKLLLEAgADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLL 277
Ank_2 pfam12796
Ankyrin repeats (3 copies);
54-144 2.59e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.86  E-value: 2.59e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857  54 LFFAAQQGHNDVVKFLFEFGASTEFKNKDGGTALLAACQYGHTKVVETLLKHGANvhDQLYDGASAIFLAAQGGYLDVIR 133
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|.
gi 2024369857 134 LLLSSGAKVNQ 144
Cdd:pfam12796  79 LLLEKGADINV 89
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 42-181 2.88e-15

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 75.29  E-value: 2.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857  42 DVDCKDSSGATALFFAAQQGHNDVVKFLFEFGASTEFKNKDGGTALLAACQYGHTKVVEtLLKHGANVHDQlYDGASAIF 121
Cdd:PLN03192  550 DPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFR-ILYHFASISDP-HAAGDLLC 627

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857 122 LAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGAERDAARDD 181
Cdd:PLN03192  628 TAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTD 687
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 52-186 2.76e-07

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: 2.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857  52 TALFFAAQQGHNDVVKFLFEFgASTEFKNKD--GGTALLAACQYGHTKVVETLLKHG---AN--VHDQLYDGASAIFLAA 124
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKC-PSCDLFQRGalGETALHVAALYDNLEAAVVLMEAApelVNepMTSDLYQGETALHIAV 97

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024369857 125 QGGYLDVIRLLLSSGAKVNQPRQDGTA--------------PLWIASQMGHSEVVRVMLLRGAERDAARDDGTTAL 186
Cdd:cd22192    98 VNQNLNLVRELIARGADVVSPRATGTFfrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 22-191 4.23e-06

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: 47.77  E-value: 4.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857  22 WAARKGNLALLQLLLNSGRVDVDCKDSSGATALFFAAQQGHNDVVKFLFefgastEFKNKDG--GTALLAACQYGHTKVV 99
Cdd:TIGR00870  24 AAERGDLASVYRDLEEPKKLNINCPDRLGRSALFVAAIENENLELTELL------LNLSCRGavGDTLLHAISLEYVDAV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857 100 ETLLKHGANVH--------------DQLYDGASAIFLAAQGGYLDVIRLLLSSGAKVN----------QPRQD----GTA 151
Cdd:TIGR00870  98 EAILLHLLAAFrksgplelandqytSEFTPGITALHLAAHRQNYEIVKLLLERGASVParacgdffvkSQGVDsfyhGES 177

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2024369857 152 PLWIASQMGHSEVVRVMLLRGAERDAARDDGTTaLLKAAI 191
Cdd:TIGR00870 178 PLNAAACLGSPSIVALLSEDPADILTADSLGNT-LLHLLV 216
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 82-111 6.48e-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: 36.41  E-value: 6.48e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 2024369857   82 DGGTALLAACQYGHTKVVETLLKHGANVHD 111
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
16-239 1.57e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 144.33  E-value: 1.57e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857  16 LANAAFWAARKGNLALLQLLLNSGRVDVDCKDSSGATALFFAAQQGHNDVVKFLFEFGASTEFKNKDGGTALLAACQYGH 95
Cdd:COG0666    53 LGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGN 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857  96 TKVVETLLKHGANVHDQLYDGASAIFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGAER 175
Cdd:COG0666   133 LEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADV 212

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024369857 176 DAARDDGTTALLKAAIKGYNNVIEELLKF-SPTLGLLKNGTSALHAAVLSGNVRTVALLLEAGAD 239
Cdd:COG0666   213 NAKDNDGKTALDLAAENGNLEIVKLLLEAgADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLL 277
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
16-271 5.02e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 135.08  E-value: 5.02e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857  16 LANAAFWAARKGNLALLQLLLNSGRVDVDCKDSSGATALFFAAQQGHNDVVKFLFEFGASTEFKNKDGGTALLAACQYGH 95
Cdd:COG0666    20 LLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGD 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857  96 TKVVETLLKHGANVHDQLYDGASAIFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGAER 175
Cdd:COG0666   100 LEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADV 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857 176 DAARDDGTTALLKAAIKGYNNVIEELLKFSPTLGLL-KNGTSALHAAVLSGNVRTVALLLEAGADPCLRNKANELPAELT 254
Cdd:COG0666   180 NARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKdNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLA 259

                         250
                  ....*....|....*..
gi 2024369857 255 KNERILRLLRTKEKQRK 271
Cdd:COG0666   260 AAAGAALIVKLLLLALL 276
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
42-271 5.94e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 121.98  E-value: 5.94e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857  42 DVDCKDSSGATALFFAAQQGHNDVVKFLFEFGASTEFKNKDGGTALLAACQYGHTKVVETLLKHGANVHDQLYDGASAIF 121
Cdd:COG0666    13 AALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLH 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857 122 LAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGAERDAARDDGTTALLKAAIKGYNNVIEEL 201
Cdd:COG0666    93 AAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024369857 202 LKFSPTLGLL-KNGTSALHAAVLSGNVRTVALLLEAGADPCLRNKANELPAELTKNERILRLLRTKEKQRK 271
Cdd:COG0666   173 LEAGADVNARdNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
18-186 3.09e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 109.27  E-value: 3.09e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857  18 NAAFWAARKGNLALLQLLLNSGrVDVDCKDSSGATALFFAAQQGHNDVVKFLFEFGASTEFKNKDGGTALLAACQYGHTK 97
Cdd:COG0666   122 TPLHLAAYNGNLEIVKLLLEAG-ADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLE 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857  98 VVETLLKHGANVHDQLYDGASAIFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGAERDA 177
Cdd:COG0666   201 IVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAA 280


                  ....*....
gi 2024369857 178 ARDDGTTAL 186
Cdd:COG0666   281 ALLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
54-144 2.59e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.86  E-value: 2.59e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857  54 LFFAAQQGHNDVVKFLFEFGASTEFKNKDGGTALLAACQYGHTKVVETLLKHGANvhDQLYDGASAIFLAAQGGYLDVIR 133
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|.
gi 2024369857 134 LLLSSGAKVNQ 144
Cdd:pfam12796  79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
153-244 1.05e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 73.23  E-value: 1.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857 153 LWIASQMGHSEVVRVMLLRGAERDAARDDGTTALLKAAIKGYNNVIEELLKFsPTLGLLKNGTSALHAAVLSGNVRTVAL 232
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGRTALHYAARSGHLEIVKL 79

                          90
                  ....*....|..
gi 2024369857 233 LLEAGADPCLRN 244
Cdd:pfam12796  80 LLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
87-174 7.76e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.92  E-value: 7.76e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857  87 LLAACQYGHTKVVETLLKHGANVHDQLYDGASAIFLAAQGGYLDVIRLLLSSGAKVNQPrqDGTAPLWIASQMGHSEVVR 166
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD--NGRTALHYAARSGHLEIVK 78


                  ....*...
gi 2024369857 167 VMLLRGAE 174
Cdd:pfam12796  79 LLLEKGAD 86
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 42-181 2.88e-15

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 75.29  E-value: 2.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857  42 DVDCKDSSGATALFFAAQQGHNDVVKFLFEFGASTEFKNKDGGTALLAACQYGHTKVVEtLLKHGANVHDQlYDGASAIF 121
Cdd:PLN03192  550 DPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFR-ILYHFASISDP-HAAGDLLC 627

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857 122 LAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGAERDAARDD 181
Cdd:PLN03192  628 TAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTD 687
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 97-263 1.58e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 72.78  E-value: 1.58e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857  97 KVVETLLKHGANVHDQLYDGASAIFLAAQGGY-----LDVIRLLLSSGAKVNQPRQDGTAPLWIASQ--MGHSEVVRVML 169
Cdd:PHA03100   49 DVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITPLLYAISkkSNSYSIVEYLL 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857 170 LRGAERDAARDDGTTAL-------------LKAAI-KGYN----NVIEELLKF-SPTLGLLKNGTSALHAAVLSGNVRTV 230
Cdd:PHA03100  129 DNGANVNIKNSDGENLLhlylesnkidlkiLKLLIdKGVDinakNRVNYLLSYgVPINIKDVYGFTPLHYAVYNNNPEFV 208

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2024369857 231 ALLLEAGADPCLRNKANELPAE---LTKNERILRLL 263
Cdd:PHA03100  209 KYLLDLGANPNLVNKYGDTPLHiaiLNNNKEIFKLL 244
Ank_2 pfam12796
Ankyrin repeats (3 copies);
21-112 1.89e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.06  E-value: 1.89e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857  21 FWAARKGNLALLQLLLNSGrVDVDCKDSSGATALFFAAQQGHNDVVKFLFEFGASTEfkNKDGGTALLAACQYGHTKVVE 100
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 2024369857 101 TLLKHGANVHDQ 112
Cdd:pfam12796  79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
120-203 1.99e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.06  E-value: 1.99e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857 120 IFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVmLLRGAERDaARDDGTTALLKAAIKGYNNVIE 199
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKL-LLEHADVN-LKDNGRTALHYAARSGHLEIVK 78


                  ....
gi 2024369857 200 ELLK 203
Cdd:pfam12796  79 LLLE 82
PHA03095 PHA03095
ankyrin-like protein; Provisional
 42-266 2.84e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 71.98  E-value: 2.84e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857  42 DVDCKDSSGATALFFAAQQGHN-DVVKFLFEFGASTEFKNKDGGTALlAACQYG---HTKVVETLLKHGANVHDQLYDGA 117
Cdd:PHA03095   75 DVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGADVNAKDKVGRTPL-HVYLSGfniNPKVIRLLLRKGADVNALDLYGM 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857 118 S--AIFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHS--EVVRVMLLRGAERDAARDDGTTALLKAAIKG 193
Cdd:PHA03095  154 TplAVLLKSRNANVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLHSMATGS 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857 194 Y--NNVIEELLKFSPTLGLL-KNGTSALHAAVLSGNVRTVALLLEAGADPCLRNKANELPAELT---KNERILRL-LRTK 266
Cdd:PHA03095  234 SckRSLVLPLLIAGISINARnRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMvrnNNGRAVRAaLAKN 313
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 61-240 2.46e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 69.25  E-value: 2.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857  61 GHNDVVKFLFEFGASTEFKNKDGGTALLAACQYGHTKVVETLLKHGANVHDQLYDGASAIFLAAQGGYLDVIRLLLSSGA 140
Cdd:PHA02875   13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857 141 KVNQP-RQDGTAPLWIASQMGHSEVVRVMLLRGAERDAARDDGTTALLKAAIKGYNNVIEELLKFSPTLGLLKN-GTSAL 218
Cdd:PHA02875   93 FADDVfYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCcGCTPL 172

                         170       180
                  ....*....|....*....|..
gi 2024369857 219 HAAVLSGNVRTVALLLEAGADP 240
Cdd:PHA02875  173 IIAMAKGDIAICKMLLDSGANI 194
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 4-250 7.88e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 67.68  E-value: 7.88e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857   4 GWCVTIGSKET--PLANAAfwaaRKGNLALLQLLLNSGrVDVDCKDSSGATALFFAAQQGHNDVVKFLFEFGASTEF--- 78
Cdd:PHA02874   25 GNCINISVDETttPLIDAI----RSGDAKIVELFIKHG-ADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSIlpi 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857  79 --------------------KNKDGGTALLAACQYGHTKVVETLLKHGANVHDQLYDGASAIFLAAQGGYLDVIRLLLSS 138
Cdd:PHA02874  100 pciekdmiktildcgidvniKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEK 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857 139 GAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGAERDAARDDGTTALLKAAIkgYNNVIEELLKFSPTLGLLK-NGTSA 217
Cdd:PHA02874  180 GAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDiDGSTP 257

                         250       260       270
                  ....*....|....*....|....*....|....
gi 2024369857 218 LHAAV-LSGNVRTVALLLEAGADPCLRNKANELP 250
Cdd:PHA02874  258 LHHAInPPCDIDIIDILLYHKADISIKDNKGENP 291
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 50-239 1.21e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 67.32  E-value: 1.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857  50 GATALFFAAQQGHNDVVKFLFEFGASTEFKNKDGGTALLAACQYGHTKVVETLLKHGANVHDQLY-DGASAIFLAAQGGY 128
Cdd:PHA02875   35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYkDGMTPLHLATILKK 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857 129 LDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGAERDAARDDGTTALLKAAIKGYNNVIEELLKFSPTL 208
Cdd:PHA02875  115 LDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANI 194

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2024369857 209 GLL-KNG-TSALHAAVLSGNVRTVALLLEAGAD 239
Cdd:PHA02875  195 DYFgKNGcVAALCYAIENNKIDIVRLFIKRGAD 227
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 41-207 1.53e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 63.92  E-value: 1.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857  41 VDVDCKDSSGATALFFAAQQ--GHNDVVKFLFEFGASTEFKNKDGGTALLAACQYGH--TKVVETLLKHGANVHDqlydg 116
Cdd:PHA03100   97 ANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINA----- 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857 117 asaiflaaqggyLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGAERDAARDDGTTALLKAAIKGYNN 196
Cdd:PHA03100  172 ------------KNRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKE 239

                         170
                  ....*....|.
gi 2024369857 197 VIEELLKFSPT 207
Cdd:PHA03100  240 IFKLLLNNGPS 250
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 96-250 2.61e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 60.28  E-value: 2.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857  96 TKVVETLLKHGANVHDQLYD-GASAIFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGAE 174
Cdd:PHA02878  147 AEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS 226

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857 175 RDAARDDGTTALLKAA--IKGYnNVIEELLKF-------SPTLGLlkngtSALHAAVLSGnvRTVALLLEAGADPCLRNK 245
Cdd:PHA02878  227 TDARDKCGNTPLHISVgyCKDY-DILKLLLEHgvdvnakSYILGL-----TALHSSIKSE--RKLKLLLEYGADINSLNS 298


                  ....*
gi 2024369857 246 ANELP 250
Cdd:PHA02878  299 YKLTP 303
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 39-250 6.07e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 59.31  E-value: 6.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857  39 GRVDVDCKDSSGATALFFAAQQGHNDVVKFLFEFGASTEFKNKDGGTALLAACQYGHTKVVETLLKHGANVHDQLYDGAS 118
Cdd:PHA02876  167 GGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNDLSLLK 246

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857 119 AIflaaQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGH-SEVVRVMLLRGAERDAARDDGTTALLKAAIKGYNNv 197
Cdd:PHA02876  247 AI----RNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYDT- 321

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024369857 198 ieELLKFSPTLGLLKNGTSALH------AAVLSGNVRTVALLLEAGADPCLRNKANELP 250
Cdd:PHA02876  322 --ENIRTLIMLGADVNAADRLYitplhqASTLDRNKDIVITLLELGANVNARDYCDKTP 378
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 42-177 9.17e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 58.92  E-value: 9.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857  42 DVDCKDSSGATALFFAAQQGHNDVVKFLFEFGASTEFKNKDGGTAL-LAACQYGHTKVVETLLKHGANVHDQLYDGASAI 120
Cdd:PHA02876  367 NVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALhFALCGTNPYMSVKTLIDRGANVNSKNKDLSTPL 446

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024369857 121 FLAAQGG-YLDVIRLLLSSGAKVNQPRQDGTAPLWIAsqMGHSEVVRVMLLRGAE-RDA 177
Cdd:PHA02876  447 HYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIA--LEYHGIVNILLHYGAElRDS 503
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 42-174 1.64e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 57.69  E-value: 1.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857  42 DVDCKDssGATALFFAAQQGHNDVVKFLFEFGASTEFKNKDGGTALLAACQYGHTKVVETLLKHGANVHDQLYDGASAIF 121
Cdd:PHA02875   96 DVFYKD--GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLI 173

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2024369857 122 LAAQGGYLDVIRLLLSSGAKVNQPRQDG-TAPLWIASQMGHSEVVRVMLLRGAE 174
Cdd:PHA02875  174 IAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGAD 227
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 122-205 2.22e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.60  E-value: 2.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857 122 LAAQGGYLDvIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGAERDAARDDGTTALLKAAIKGYNNVIEEL 201
Cdd:PTZ00322   89 LAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167


                  ....
gi 2024369857 202 LKFS 205
Cdd:PTZ00322  168 SRHS 171
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 41-250 2.52e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 57.28  E-value: 2.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857  41 VDVDCKDSSGATALFFAAQQGHNDVVKFLFEFGASTEFKNKDGGTALLAACQYGHTKVVETLLKHGA--NVHDqlYDGAS 118
Cdd:PHA02874  115 IDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAyaNVKD--NNGES 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857 119 AIFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIAsqMGHSEVVRVMLLRGAERDAARDDGTTALLKAAIKGYN-NV 197
Cdd:PHA02874  193 PLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA--IIHNRSAIELLINNASINDQDIDGSTPLHHAINPPCDiDI 270

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2024369857 198 IEELLKFSPTLGLLKN-GTSALHAAVlsGNVRTVALLLEAGADPCLRNKANELP 250
Cdd:PHA02874  271 IDILLYHKADISIKDNkGENPIDTAF--KYINKDPVIKDIIANAVLIKEADKLK 322
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 38-130 6.35e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.45  E-value: 6.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857  38 SGRVDVDCKDSSGATALFFAAQQGHNDVVKFLFEFGASTEFKNKDGGTALLAACQYGHTKVVETLLKHGANVHDQLYDGA 117
Cdd:PTZ00322  103 TGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGANAK 182

                          90
                  ....*....|...
gi 2024369857 118 SAIFLAAQGGYLD 130
Cdd:PTZ00322  183 PDSFTGKPPSLED 195
Ank_4 pfam13637
Ankyrin repeats (many copies);
83-136 8.88e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.74  E-value: 8.88e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2024369857  83 GGTALLAACQYGHTKVVETLLKHGANVHDQLYDGASAIFLAAQGGYLDVIRLLL 136
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 64-241 2.28e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 54.26  E-value: 2.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857  64 DVVKFLFEFGASTEFKNKDGGTALlaaCQYGHT------KVVETLLKHGANVHDQLYDGASAIFLAAQGGY-LDVIRLLL 136
Cdd:PHA03095   28 EEVRRLLAAGADVNFRGEYGKTPL---HLYLHYssekvkDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLI 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857 137 SSGAKVNQPRQDGTAPLWI--ASQMGHSEVVRVMLLRGAERDAARDDGTTALlkaAIkgynnvieellkfsptlgLLKNg 214
Cdd:PHA03095  105 KAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPL---AV------------------LLKS- 162

                         170       180
                  ....*....|....*....|....*..
gi 2024369857 215 tsalHAAvlsgNVRTVALLLEAGADPC 241
Cdd:PHA03095  163 ----RNA----NVELLRLLIDAGADVY 181
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 127-263 2.77e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 54.23  E-value: 2.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857 127 GYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGAERDAARDDGTTALLKAAIKGYNNVIEELL---K 203
Cdd:PHA02875   13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLdlgK 92

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024369857 204 FSPTLgLLKNGTSALHAAVLSGNVRTVALLLEAGADPCLRNKANELP---AELTKNERILRLL 263
Cdd:PHA02875   93 FADDV-FYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPlhlAVMMGDIKGIELL 154
Ank_4 pfam13637
Ankyrin repeats (many copies);
52-103 2.97e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.20  E-value: 2.97e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2024369857  52 TALFFAAQQGHNDVVKFLFEFGASTEFKNKDGGTALLAACQYGHTKVVETLL 103
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 52-186 2.76e-07

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: 2.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857  52 TALFFAAQQGHNDVVKFLFEFgASTEFKNKD--GGTALLAACQYGHTKVVETLLKHG---AN--VHDQLYDGASAIFLAA 124
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKC-PSCDLFQRGalGETALHVAALYDNLEAAVVLMEAApelVNepMTSDLYQGETALHIAV 97

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024369857 125 QGGYLDVIRLLLSSGAKVNQPRQDGTA--------------PLWIASQMGHSEVVRVMLLRGAERDAARDDGTTAL 186
Cdd:cd22192    98 VNQNLNLVRELIARGADVVSPRATGTFfrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 42-194 7.21e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 49.88  E-value: 7.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857  42 DVDCKD-SSGATALFFAAQQGHNDVVKFLFEFGASTEFKNKDGGTALLAACQYGHTKVVETLLKHGANVHDQLYDGASAI 120
Cdd:PHA02878  159 DINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPL 238

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024369857 121 FLAAqgGYL---DVIRLLLSSGAKVN-QPRQDGTAPLWIASqmgHSE-VVRVMLLRGAERDAARDDGTTALLKAAIKGY 194
Cdd:PHA02878  239 HISV--GYCkdyDILKLLLEHGVDVNaKSYILGLTALHSSI---KSErKLKLLLEYGADINSLNSYKLTPLSSAVKQYL 312
PHA03095 PHA03095
ankyrin-like protein; Provisional
 128-263 2.17e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 48.48  E-value: 2.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857 128 YLDVIRLLLSSGAKVNQPRQDGTAPLwiaSQMGHS------EVVRVMLLRGAERDAARDDGTTALLKAAikgYNNVIEEL 201
Cdd:PHA03095   26 TVEEVRRLLAAGADVNFRGEYGKTPL---HLYLHYssekvkDIVRLLLEAGADVNAPERCGFTPLHLYL---YNATTLDV 99

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024369857 202 LKFsptlgLLKNGTS----------ALHA--AVLSGNVRTVALLLEAGADPCLRNKANELP-AELTKNER----ILRLL 263
Cdd:PHA03095  100 IKL-----LIKAGADvnakdkvgrtPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPlAVLLKSRNanveLLRLL 173
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 22-250 2.88e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.14  E-value: 2.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857  22 WAARKGNLALLQLLLNSGrVDVDCKDSSGATALFFAAQQGHNDVVKFLFEFGASTE---------FKNKDGGTALL---- 88
Cdd:PHA02876  184 YAAERGNAKMVNLLLSYG-ADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINkndlsllkaIRNEDLETSLLlyda 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857  89 -----------------AACQYGHTKVVETLLKHGANVHDQLYDGASAIFLAAQGGY-LDVIRLLLSSGAKVNQPRQDGT 150
Cdd:PHA02876  263 gfsvnsiddckntplhhASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYI 342

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857 151 APLWIASQMG-HSEVVRVMLLRGAERDAARDDGTTALLKAAIKGYNNVIEELLKFSPTLGLL--KNGTsALHAAVLSGNV 227
Cdd:PHA02876  343 TPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALsqKIGT-ALHFALCGTNP 421

                         250       260
                  ....*....|....*....|....
gi 2024369857 228 RT-VALLLEAGADPCLRNKANELP 250
Cdd:PHA02876  422 YMsVKTLIDRGANVNSKNKDLSTP 445
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 42-143 3.14e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 47.68  E-value: 3.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857  42 DVDCKDSSGATALFFAAQQGHNDVVKFLFEFGASTEFKNKDGGTALLAACQYGHTKVVETLLKHGANVHDQLYDG-ASAI 120
Cdd:PHA02875  127 DPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAAL 206

                          90       100
                  ....*....|....*....|...
gi 2024369857 121 FLAAQGGYLDVIRLLLSSGAKVN 143
Cdd:PHA02875  207 CYAIENNKIDIVRLFIKRGADCN 229
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 22-191 4.23e-06

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: 47.77  E-value: 4.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857  22 WAARKGNLALLQLLLNSGRVDVDCKDSSGATALFFAAQQGHNDVVKFLFefgastEFKNKDG--GTALLAACQYGHTKVV 99
Cdd:TIGR00870  24 AAERGDLASVYRDLEEPKKLNINCPDRLGRSALFVAAIENENLELTELL------LNLSCRGavGDTLLHAISLEYVDAV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857 100 ETLLKHGANVH--------------DQLYDGASAIFLAAQGGYLDVIRLLLSSGAKVN----------QPRQD----GTA 151
Cdd:TIGR00870  98 EAILLHLLAAFrksgplelandqytSEFTPGITALHLAAHRQNYEIVKLLLERGASVParacgdffvkSQGVDsfyhGES 177

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2024369857 152 PLWIASQMGHSEVVRVMLLRGAERDAARDDGTTaLLKAAI 191
Cdd:TIGR00870 178 PLNAAACLGSPSIVALLSEDPADILTADSLGNT-LLHLLV 216
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 66-137 5.35e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.20  E-value: 5.35e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024369857  66 VKFLFEFGASTEFKNKDGGTALLAACQYGHTKVVETLLKHGANVHDQLYDGASAIFLAAQGGYLDVIRLLLS 137
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 41-109 5.37e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 46.97  E-value: 5.37e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024369857  41 VDVDCKDSSGATALFFAAQQGHNDVVKFLFEFGASTEFKNKDGGTALLAACQYGHTKVVETLLKHGANV 109
Cdd:PHA03100  183 VPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSI 251
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 88-169 5.59e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.20  E-value: 5.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857  88 LAACqyGHTKVVETLLKHGANVHDQLYDGASAIFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRV 167
Cdd:PTZ00322   89 LAAS--GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                  ..
gi 2024369857 168 ML 169
Cdd:PTZ00322  167 LS 168
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 64-143 6.92e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 46.58  E-value: 6.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857  64 DVVKFLFEFGASTEFKNKDGGTALLAACQYGHTKVVETLLKHGANVHDQLYDGASAIFLAAQGGYLDVIRLLLSSGAKVN 143
Cdd:PHA03100  173 NRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
Ank_4 pfam13637
Ankyrin repeats (many copies);
118-169 1.38e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.49  E-value: 1.38e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2024369857 118 SAIFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVML 169
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 41-202 2.06e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.44  E-value: 2.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857  41 VDVDCKDSSGATALFFAAQQGHN-DVVKFLFEFGASTEFKNKDGGTALLAACQYGHTK-VVETLLKHGANVHDQLYDGAS 118
Cdd:PHA02876  298 ADVNAKNIKGETPLYLMAKNGYDtENIRTLIMLGADVNAADRLYITPLHQASTLDRNKdIVITLLELGANVNARDYCDKT 377

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857 119 AIFLAAQGGYLDVIRLLLSSGAKVNQPRQD-GTAPLWIASQMGHSEVVRVMLLRGAERDAARDDGTTALLKAAIKGYN-N 196
Cdd:PHA02876  378 PIHYAAVRNNVVIINTLLDYGADIEALSQKiGTALHFALCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKlD 457


                  ....*.
gi 2024369857 197 VIEELL 202
Cdd:PHA02876  458 VIEMLL 463
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 100-263 7.93e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 43.72  E-value: 7.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857 100 ETLLKH--GANVHDQLYDGASAIFL-----AAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIA----SQMGHSEVVRVM 168
Cdd:PHA02878   14 ETILKYieYIDHTENYSTSASLIPFiplhqAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIIckepNKLGMKEMIRSI 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857 169 LLRG---AER-------------------DAARDDGTTALLKAAIKGYNNVIE-ELLKFSPTLGLLKN------GTSALH 219
Cdd:PHA02878   94 NKCSvfyTLVaikdafnnrnveifkiiltNRYKNIQTIDLVYIDKKSKDDIIEaEITKLLLSYGADINmkdrhkGNTALH 173

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2024369857 220 AAVLSGNVRTVALLLEAGADPCLRNKANELP---AELTKNERILRLL 263
Cdd:PHA02878  174 YATENKDQRLTELLLSYGANVNIPDKTNNSPlhhAVKHYNKPIVHIL 220
Ank_5 pfam13857
Ankyrin repeats (many copies);
39-87 8.46e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.64  E-value: 8.46e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2024369857  39 GRVDVDCKDSSGATALFFAAQQGHNDVVKFLFEFGASTEFKNKDGGTAL 87
Cdd:pfam13857   5 GPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 213-245 9.86e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.81  E-value: 9.86e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2024369857 213 NGTSALHAAVLS-GNVRTVALLLEAGADPCLRNK 245
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 82-112 1.15e-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: 38.42  E-value: 1.15e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2024369857  82 DGGTAL-LAACQYGHTKVVETLLKHGANVHDQ 112
Cdd:pfam00023   1 DGNTPLhLAAGRRGNLEIVKLLLSKGADVNAR 32
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 182-263 2.21e-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: 42.17  E-value: 2.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857 182 GTTALLKAAI---KGYNNVIEELLKFSPTLGLLKN------------GTSALHAAVLSGNVRTVALLLEAGADPCLRNKA 246
Cdd:cd21882    26 GKTCLHKAALnlnDGVNEAIMLLLEAAPDSGNPKElvnapctdefyqGQTALHIAIENRNLNLVRLLVENGADVSARATG 105

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2024369857 247 N-------------ELP---AELTKNERILRLL 263
Cdd:cd21882   106 RffrkspgnlfyfgELPlslAACTNQEEIVRLL 138
PHA02798 PHA02798
ankyrin-like protein; Provisional
 64-144 2.90e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 41.74  E-value: 2.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857  64 DVVKFLFEFGASTEFKNKDGGTALLAACQYGHTKVVETLL---KHGANVHDQLYDGASAIFLAAQGGY---LDVIRLLLS 137
Cdd:PHA02798   90 DIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLfmiENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLE 169


                  ....*..
gi 2024369857 138 SGAKVNQ 144
Cdd:PHA02798  170 KGVDINT 176
PHA02798 PHA02798
ankyrin-like protein; Provisional
 96-203 3.17e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 41.74  E-value: 3.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857  96 TKVVETLLKHGANVH--DQLYDGASAIFLAAQGGY---LDVIRLLLSSGAKVNQPRQDGTAPLWIA---SQMGHSEVVRV 167
Cdd:PHA02798   51 TDIVKLFINLGANVNglDNEYSTPLCTILSNIKDYkhmLDIVKILIENGADINKKNSDGETPLYCLlsnGYINNLEILLF 130

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2024369857 168 MLLRGAERDAARDDGTTaLLKAAIKGYNNVIEELLK 203
Cdd:PHA02798  131 MIENGADTTLLDKDGFT-MLQVYLQSNHHIDIEIIK 165
Ank_4 pfam13637
Ankyrin repeats (many copies);
182-234 5.98e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.25  E-value: 5.98e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2024369857 182 GTTALLKAAIKGYNNVIEELLKFSPTLGLL-KNGTSALHAAVLSGNVRTVALLL 234
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVdGNGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 82-111 6.48e-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: 36.41  E-value: 6.48e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 2024369857   82 DGGTALLAACQYGHTKVVETLLKHGANVHD 111
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_2 pfam12796
Ankyrin repeats (3 copies);
18-80 6.57e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 38.17  E-value: 6.57e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024369857  18 NAAFWAARKGNLALLQLLLNSGRVDVDCKdssGATALFFAAQQGHNDVVKFLFEFGASTEFKN 80
Cdd:pfam12796  32 TALHLAAKNGHLEIVKLLLEHADVNLKDN---GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
Ank_4 pfam13637
Ankyrin repeats (many copies);
18-69 9.23e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.48  E-value: 9.23e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2024369857  18 NAAFWAARKGNLALLQLLLNSGrVDVDCKDSSGATALFFAAQQGHNDVVKFL 69
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKG-ADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 82-110 1.53e-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: 35.31  E-value: 1.53e-03
                          10        20
                  ....*....|....*....|....*....
gi 2024369857  82 DGGTALLAACQYGHTKVVETLLKHGANVH 110
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
Ank_4 pfam13637
Ankyrin repeats (many copies);
214-263 1.60e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 35.71  E-value: 1.60e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2024369857 214 GTSALHAAVLSGNVRTVALLLEAGADPCLRNKANELP---AELTKNERILRLL 263
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETAlhfAASNGNVEVLKLL 53
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 88-250 1.72e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 39.56  E-value: 1.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857  88 LAACQY-GHTKVVETLLKHGAN-VHDQLYDGASAIFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVV 165
Cdd:PHA02874    5 LRMCIYsGDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDII 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857 166 RVMLLRGA----------ERDA------------ARDDGTTALLKAAIK-GYNNVIEELLKFSPTLGLLK-NGTSALHAA 221
Cdd:PHA02874   85 KLLIDNGVdtsilpipciEKDMiktildcgidvnIKDAELKTFLHYAIKkGDLESIKMLFEYGADVNIEDdNGCYPIHIA 164

                         170       180
                  ....*....|....*....|....*....
gi 2024369857 222 VLSGNVRTVALLLEAGADPCLRNKANELP 250
Cdd:PHA02874  165 IKHNFFDIIKLLLEKGAYANVKDNNGESP 193
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 83-235 2.05e-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: 39.48  E-value: 2.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857  83 GGTALLAACQYGHTKVVETL------------LKHGANVH--DQLYDGASAIFLAAQGGYLDVIRLLLSSGAKVnQPRQD 148
Cdd:cd21882    26 GKTCLHKAALNLNDGVNEAImllleaapdsgnPKELVNAPctDEFYQGQTALHIAIENRNLNLVRLLVENGADV-SARAT 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857 149 GTA--------------PLWIASQMGHSEVVRVMLLRGAERDA--ARD--------------DGTTALLKAAIKGYNNVI 198
Cdd:cd21882   105 GRFfrkspgnlfyfgelPLSLAACTNQEEIVRLLLENGAQPAAleAQDslgntvlhalvlqaDNTPENSAFVCQMYNLLL 184

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2024369857 199 EELLKFSPT--LGLLKN--GTSALHAAVLSGNVRTVALLLE 235
Cdd:cd21882   185 SYGAHLDPTqqLEEIPNhqGLTPLKLAAVEGKIVMFQHILQ 225
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 118-239 2.25e-03

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 39.23  E-value: 2.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857 118 SAIFLAAQGGYLDVI-RLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLlrgaerDAARDdgttallkaaikgynn 196
Cdd:cd22192    19 SPLLLAAKENDVQAIkKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLM------EAAPE---------------- 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2024369857 197 vieelLKFSPTLGLLKNGTSALHAAVLSGNVRTVALLLEAGAD 239
Cdd:cd22192    77 -----LVNEPMTSDLYQGETALHIAVVNQNLNLVRELIARGAD 114
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 213-253 3.39e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 38.73  E-value: 3.39e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2024369857 213 NGTSALHAAVLSGNVRTVALLLEAGADPCLRNKANELPAEL 253
Cdd:PTZ00322  114 DGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLEL 154
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 213-240 3.77e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.10  E-value: 3.77e-03
                           10        20
                   ....*....|....*....|....*...
gi 2024369857  213 NGTSALHAAVLSGNVRTVALLLEAGADP 240
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 182-239 3.82e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 38.63  E-value: 3.82e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024369857 182 GTTALLKAAI---KGYNNVIEELLKFSPTLGLLKN------------GTSALHAAVLSGNVRTVALLLEAGAD 239
Cdd:cd22196    47 GKTCLLKAMLnlhNGQNDTISLLLDIAEKTGNLKEfvnaaytdsyykGQTALHIAIERRNMHLVELLVQNGAD 119
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 115-143 4.08e-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: 34.10  E-value: 4.08e-03
                           10        20
                   ....*....|....*....|....*....
gi 2024369857  115 DGASAIFLAAQGGYLDVIRLLLSSGAKVN 143
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 92-260 4.61e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 38.12  E-value: 4.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857  92 QYGHTKVVETLLKHGANVHDQLYDGASAIFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLlr 171
Cdd:PHA02876  154 QQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII-- 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024369857 172 gaERDAARDDGTTALLKAAikgYNNVIEELL-----KFS-PTLGLLKNgtSALHAAVLSGNV-RTVALLLEAGADPCLRN 244
Cdd:PHA02876  232 --DNRSNINKNDLSLLKAI---RNEDLETSLllydaGFSvNSIDDCKN--TPLHHASQAPSLsRLVPKLLERGADVNAKN 304

                         170       180
                  ....*....|....*....|...
gi 2024369857 245 KANELPAEL-------TKNERIL 260
Cdd:PHA02876  305 IKGETPLYLmakngydTENIRTL 327
 
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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