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Conserved domains on  [gi|268370076|ref|NP_001161229|]
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ankyrin repeat domain-containing protein 7 isoform 1 [Mus musculus]

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];
25-258 8.66e-43

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 147.79  E-value: 8.66e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076  25 ISLAKTAPPSLSIGGGYHLRDKHLKKLHKAATIGNEQKLKDYLERKKYNVNGRDKRSRTPLHLACANGYTNIVSLLIENQ 104
Cdd:COG0666   31 LLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAG 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076 105 CKINVQDSENRTPLIKqAVECQQESCATVLLLHGADPNLVDVYSNTALHYAVCGQNISLANKLLQYKANLEAKNKDGHTP 184
Cdd:COG0666  111 ADVNARDKDGETPLHL-AAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETP 189
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 268370076 185 LLLAVAENNENMVKFLLKKGADVNASDKNHRTAIMIALIVEPTSSVKLLLQQDTDLAHKDIYGFTAEEYASFNG 258
Cdd:COG0666  190 LHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAG 263
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
25-258 8.66e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 147.79  E-value: 8.66e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076  25 ISLAKTAPPSLSIGGGYHLRDKHLKKLHKAATIGNEQKLKDYLERKKYNVNGRDKRSRTPLHLACANGYTNIVSLLIENQ 104
Cdd:COG0666   31 LLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAG 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076 105 CKINVQDSENRTPLIKqAVECQQESCATVLLLHGADPNLVDVYSNTALHYAVCGQNISLANKLLQYKANLEAKNKDGHTP 184
Cdd:COG0666  111 ADVNARDKDGETPLHL-AAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETP 189
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 268370076 185 LLLAVAENNENMVKFLLKKGADVNASDKNHRTAIMIALIVEPTSSVKLLLQQDTDLAHKDIYGFTAEEYASFNG 258
Cdd:COG0666  190 LHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAG 263
PHA03100 PHA03100
ankyrin repeat protein; Provisional
51-235 1.03e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 88.18  E-value: 1.03e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076  51 LHKAATIGNEQKLKdYLERKKYNVNGRDKRSRTPLHLACANGYT-----NIVSLLIENQCKINVQDSENRTPLIKQAVEC 125
Cdd:PHA03100  39 LYLAKEARNIDVVK-ILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKK 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076 126 -QQESCATVLLLHGADPNLVDVYSNTALHYAV--CGQNISLANKLLQYKANLEAKN--------------KD--GHTPLL 186
Cdd:PHA03100 118 sNSYSIVEYLLDNGANVNIKNSDGENLLHLYLesNKIDLKILKLLIDKGVDINAKNrvnyllsygvpiniKDvyGFTPLH 197
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 268370076 187 LAVAENNENMVKFLLKKGADVNASDKNHRTAIMIALIVEPTSSVKLLLQ 235
Cdd:PHA03100 198 YAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLN 246
Ank_2 pfam12796
Ankyrin repeats (3 copies);
85-211 2.66e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 69.76  E-value: 2.66e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076   85 LHLACANGYTNIVSLLIENqckinvqdsenrtplikqavecqqescatvlllhGADPNLVDVYSNTALHYAVCGQNISLA 164
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLEN----------------------------------GADANLQDKNGRTALHLAAKNGHLEIV 46
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 268370076  165 nKLLQYKANLEAKNkDGHTPLLLAVAENNENMVKFLLKKGADVNASD 211
Cdd:pfam12796  47 -KLLLEHADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
131-241 1.59e-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: 48.86  E-value: 1.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076 131 ATVLLLHGAdPNLV------DVYSN-TALHYAVCGQNISLANKLLQYKANLEA---------KNKD-----GHTPLLLAV 189
Cdd:cd22192   66 AAVVLMEAA-PELVnepmtsDLYQGeTALHIAVVNQNLNLVRELIARGADVVSpratgtffrPGPKnliyyGEHPLSFAA 144
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 268370076 190 AENNENMVKFLLKKGADVNASDKNHRTAIMIaliveptssvkLLLQQDTDLA 241
Cdd:cd22192  145 CVGNEEIVRLLIEHGADIRAQDSLGNTVLHI-----------LVLQPNKTFA 185
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
49-209 6.31e-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: 47.38  E-value: 6.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076   49 KKLHKAATIGNEQKLKDYL-ERKKYNVNGRDKRSRTPL-HLACANGYTNIVSLLIENQCKINVQDSenrtplikqavecq 126
Cdd:TIGR00870  19 KAFLPAAERGDLASVYRDLeEPKKLNINCPDRLGRSALfVAAIENENLELTELLLNLSCRGAVGDT-------------- 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076  127 qescatvlLLHGADPNLVDVYSNTALH---YAVCGQNISLANKllQYKANLEAknkdGHTPLLLAVAENNENMVKFLLKK 203
Cdd:TIGR00870  85 --------LLHAISLEYVDAVEAILLHllaAFRKSGPLELAND--QYTSEFTP----GITALHLAAHRQNYEIVKLLLER 150

                  ....*.
gi 268370076  204 GADVNA 209
Cdd:TIGR00870 151 GASVPA 156
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
180-209 1.64e-05

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: 41.03  E-value: 1.64e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 268370076   180 DGHTPLLLAVAENNENMVKFLLKKGADVNA 209
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
25-258 8.66e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 147.79  E-value: 8.66e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076  25 ISLAKTAPPSLSIGGGYHLRDKHLKKLHKAATIGNEQKLKDYLERKKYNVNGRDKRSRTPLHLACANGYTNIVSLLIENQ 104
Cdd:COG0666   31 LLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAG 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076 105 CKINVQDSENRTPLIKqAVECQQESCATVLLLHGADPNLVDVYSNTALHYAVCGQNISLANKLLQYKANLEAKNKDGHTP 184
Cdd:COG0666  111 ADVNARDKDGETPLHL-AAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETP 189
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 268370076 185 LLLAVAENNENMVKFLLKKGADVNASDKNHRTAIMIALIVEPTSSVKLLLQQDTDLAHKDIYGFTAEEYASFNG 258
Cdd:COG0666  190 LHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAG 263
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
51-250 3.01e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 130.84  E-value: 3.01e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076  51 LHKAATIGNEQKLKdYLERKKYNVNGRDKRSRTPLHLACANGYTNIVSLLIENQCKINVQDSENRTPLIKqAVECQQESC 130
Cdd:COG0666   91 LHAAARNGDLEIVK-LLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL-AAANGNLEI 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076 131 ATVLLLHGADPNLVDVYSNTALHYAVCGQNISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKKGADVNAS 210
Cdd:COG0666  169 VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAK 248
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 268370076 211 DKNHRTAIMIALIVEPTSSVKLLLQQDTDLAHKDIYGFTA 250
Cdd:COG0666  249 DKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
43-258 1.21e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 126.61  E-value: 1.21e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076  43 LRDKHLKKLHKAATIGNEQKLKDYLERKKYNVNGRDKRSRTPLHLACANGYTNIVSLLIENQCKINVQDSENRTPLIkQA 122
Cdd:COG0666   16 LLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLH-AA 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076 123 VECQQESCATVLLLHGADPNLVDVYSNTALHYAVCGQNISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLK 202
Cdd:COG0666   95 ARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLE 174
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 268370076 203 KGADVNASDKNHRTAIMIALIVEPTSSVKLLLQQDTDLAHKDIYGFTAEEYASFNG 258
Cdd:COG0666  175 AGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENG 230
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
51-218 2.84e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 104.27  E-value: 2.84e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076  51 LHKAATIGNEQKLKdYLERKKYNVNGRDKRSRTPLHLACANGYTNIVSLLIENQCKINVQDSENRTPLIkQAVECQQESC 130
Cdd:COG0666  124 LHLAAYNGNLEIVK-LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLH-LAAENGHLEI 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076 131 ATVLLLHGADPNLVDVYSNTALHYAVCGQNISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKKGADVNAS 210
Cdd:COG0666  202 VKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAA 281

                 ....*...
gi 268370076 211 DKNHRTAI 218
Cdd:COG0666  282 LLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
67-258 4.03e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 103.88  E-value: 4.03e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076  67 LERKKYNVNGRDKRSRTPLHLACANGYTNIVSLLIENQCKINVQDSENRTPLIKQAVECQQESCATVLLLHGADPNLVDV 146
Cdd:COG0666    6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076 147 YSNTALHYAVCGQNISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKKGADVNASDKNHRTAIMIALIVEP 226
Cdd:COG0666   86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165
                        170       180       190
                 ....*....|....*....|....*....|..
gi 268370076 227 TSSVKLLLQQDTDLAHKDIYGFTAEEYASFNG 258
Cdd:COG0666  166 LEIVKLLLEAGADVNARDNDGETPLHLAAENG 197
PHA03100 PHA03100
ankyrin repeat protein; Provisional
51-235 1.03e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 88.18  E-value: 1.03e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076  51 LHKAATIGNEQKLKdYLERKKYNVNGRDKRSRTPLHLACANGYT-----NIVSLLIENQCKINVQDSENRTPLIKQAVEC 125
Cdd:PHA03100  39 LYLAKEARNIDVVK-ILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKK 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076 126 -QQESCATVLLLHGADPNLVDVYSNTALHYAV--CGQNISLANKLLQYKANLEAKN--------------KD--GHTPLL 186
Cdd:PHA03100 118 sNSYSIVEYLLDNGANVNIKNSDGENLLHLYLesNKIDLKILKLLIDKGVDINAKNrvnyllsygvpiniKDvyGFTPLH 197
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 268370076 187 LAVAENNENMVKFLLKKGADVNASDKNHRTAIMIALIVEPTSSVKLLLQ 235
Cdd:PHA03100 198 YAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLN 246
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
96-258 8.60e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 81.15  E-value: 8.60e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076  96 IVSLLIENQCKINVQDSENRTPLIKQAVECQQESCATVLLLHGADPNLVDVYSNTALHYAVCGQNISLANKLLQYKANLE 175
Cdd:COG0666    2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076 176 AKNKDGHTPLLLAVAENNENMVKFLLKKGADVNASDKNHRTAIMIALIVEPTSSVKLLLQQDTDLAHKDIYGFTAEEYAS 255
Cdd:COG0666   82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161

                 ...
gi 268370076 256 FNG 258
Cdd:COG0666  162 ANG 164
PHA03095 PHA03095
ankyrin-like protein; Provisional
73-254 3.54e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 80.84  E-value: 3.54e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076  73 NVNGRDKRSRTPLH--LACANG-YTNIVSLLIENQCKINVQDSENRTPLIKQAVECQQESCATVLLLHGADPNLVDVYSN 149
Cdd:PHA03095  39 DVNFRGEYGKTPLHlyLHYSSEkVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDVIKLLIKAGADVNAKDKVGR 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076 150 TALHYAVCGQNI--SLANKLLQYKANLEAKNKDGHTPLLLAVAENNEN--MVKFLLKKGADVNASDKNHRTAI-MIALIV 224
Cdd:PHA03095 119 TPLHVYLSGFNInpKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANveLLRLLIDAGADVYAVDDRFRSLLhHHLQSF 198
                        170       180       190
                 ....*....|....*....|....*....|.
gi 268370076 225 EPTSSV-KLLLQQDTDLAHKDIYGFTAEEYA 254
Cdd:PHA03095 199 KPRARIvRELIRAGCDPAATDMLGNTPLHSM 229
PHA03100 PHA03100
ankyrin repeat protein; Provisional
73-223 9.33e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 79.32  E-value: 9.33e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076  73 NVNGRDKRSRTPLHLACAN--GYTNIVSLLIENQCKINVQDSENRTPLiKQAVECQQESCATV----------------- 133
Cdd:PHA03100  98 NVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLL-HLYLESNKIDLKILkllidkgvdinaknrvn 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076 134 -LLLHGADPNLVDVYSNTALHYAVCGQNISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKKGADVNA--- 209
Cdd:PHA03100 177 yLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTiie 256
                        170
                 ....*....|....*....
gi 268370076 210 -----SDKNHRTAIMIALI 223
Cdd:PHA03100 257 tllyfKDKDLNTITKIKML 275
PHA03095 PHA03095
ankyrin-like protein; Provisional
87-250 2.22e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 78.53  E-value: 2.22e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076  87 LACANGYTNIVSLLIENQCKINVQDSENRTPLiKQAVECQQESCATV---LLLHGADPNLVDVYSNTALHYAVCGQN-IS 162
Cdd:PHA03095  20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPL-HLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHLYLYNATtLD 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076 163 LANKLLQYKANLEAKNKDGHTPL--LLAVAENNENMVKFLLKKGADVNASDKNHRTAIMIALI---VEPtSSVKLLLQQD 237
Cdd:PHA03095  99 VIKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKsrnANV-ELLRLLIDAG 177
                        170
                 ....*....|...
gi 268370076 238 TDLAHKDIYGFTA 250
Cdd:PHA03095 178 ADVYAVDDRFRSL 190
PHA02876 PHA02876
ankyrin repeat protein; Provisional
51-221 9.72e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 77.03  E-value: 9.72e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076  51 LHKAATIGNEQKLKDYLERKKYNVNGRDKRSRTPLHLACANGY-TNIVSLLIENQCKINVQDSENRTPLIKQAVECQQES 129
Cdd:PHA02876 277 LHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKD 356
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076 130 CATVLLLHGADPNLVDVYSNTALHYAVCGQNISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENM-VKFLLKKGADVN 208
Cdd:PHA02876 357 IVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVN 436
                        170
                 ....*....|...
gi 268370076 209 ASDKNHRTAIMIA 221
Cdd:PHA02876 437 SKNKDLSTPLHYA 449
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
54-211 1.03e-15

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 76.83  E-value: 1.03e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076  54 AATIGNEQKLKDYLeRKKYNVNGRDKRSRTPLHLACANGYTNIVSLLIENQCKINVQDSENRTPLIkQAVECQQESCATV 133
Cdd:PLN03192 532 VASTGNAALLEELL-KAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALW-NAISAKHHKIFRI 609
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076 134 L--LLHGADPNLvdvySNTALHYAVCGQNISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKKGADVNASD 211
Cdd:PLN03192 610 LyhFASISDPHA----AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
PHA02876 PHA02876
ankyrin repeat protein; Provisional
19-240 1.56e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 76.26  E-value: 1.56e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076  19 HSSEVPiSLAKTAPPSLSIGGGYHLRD-KHLKKLHKAATIGNEQKLKDYLERKKYNVNGRDKRSRTPLHLACA-NGYTNI 96
Cdd:PHA02876 279 HASQAP-SLSRLVPKLLERGADVNAKNiKGETPLYLMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDI 357
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076  97 VSLLIENQCKINVQDSENRTPLIKQAVEcQQESCATVLLLHGADPNLVDVYSNTALHYAVCGQNISLANK-LLQYKANLE 175
Cdd:PHA02876 358 VITLLELGANVNARDYCDKTPIHYAAVR-NNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMSVKtLIDRGANVN 436
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 268370076 176 AKNKDGHTPLLLAVAENNE-NMVKFLLKKGADVNASDKNHRTAIMIALivEPTSSVKLLLQQDTDL 240
Cdd:PHA02876 437 SKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLHYGAEL 500
Ank_2 pfam12796
Ankyrin repeats (3 copies);
85-211 2.66e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 69.76  E-value: 2.66e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076   85 LHLACANGYTNIVSLLIENqckinvqdsenrtplikqavecqqescatvlllhGADPNLVDVYSNTALHYAVCGQNISLA 164
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLEN----------------------------------GADANLQDKNGRTALHLAAKNGHLEIV 46
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 268370076  165 nKLLQYKANLEAKNkDGHTPLLLAVAENNENMVKFLLKKGADVNASD 211
Cdd:pfam12796  47 -KLLLEHADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
50-255 3.82e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 75.10  E-value: 3.82e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076  50 KLHKAATIGNEQKLKDYLERKKYNVNGRDKRSRTPLHLACANGYTNIVSLLIENQCKINV------------QDS----- 112
Cdd:PHA02876 147 KLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIialddlsvlecaVDSknidt 226
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076 113 -----ENRTPLIKQAVE----CQQESCATVLLLH--GADPNLVDVYSNTALHYAVCGQNIS-LANKLLQYKANLEAKNKD 180
Cdd:PHA02876 227 ikaiiDNRSNINKNDLSllkaIRNEDLETSLLLYdaGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIK 306
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 268370076 181 GHTPLLLaVAEN---NENmVKFLLKKGADVNASDKNHRTAIMIALIVEPTSSVKL-LLQQDTDLAHKDIYGFTAEEYAS 255
Cdd:PHA02876 307 GETPLYL-MAKNgydTEN-IRTLIMLGADVNAADRLYITPLHQASTLDRNKDIVItLLELGANVNARDYCDKTPIHYAA 383
Ank_2 pfam12796
Ankyrin repeats (3 copies);
51-145 7.18e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.60  E-value: 7.18e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076   51 LHKAATIGNEQKLKDYLErKKYNVNGRDKRSRTPLHLACANGYTNIVSLLIENqCKINVQDsENRTPLIkQAVECQQESC 130
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLE-NGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALH-YAARSGHLEI 76
                          90
                  ....*....|....*
gi 268370076  131 ATVLLLHGADPNLVD 145
Cdd:pfam12796  77 VKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
152-244 1.33e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.83  E-value: 1.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076  152 LHYAVCGQNISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKKgADVNASDkNHRTAIMIALIVEPTSSVK 231
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 268370076  232 LLLQQDTDLAHKD 244
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
66-274 4.05e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 71.98  E-value: 4.05e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076  66 YLERKKYNVNGRDKRSRTPLH--LACANGYTNIVSLLIENQCKINVQDSENRTPLIKQAVECQ-QESCATVLLLHGADPN 142
Cdd:PHA03095 137 LLLRKGADVNALDLYGMTPLAvlLKSRNANVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKpRARIVRELIRAGCDPA 216
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076 143 LVDVYSNTALHYAV--CGQNISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKKGADVNASDKNHRTAIMI 220
Cdd:PHA03095 217 ATDMLGNTPLHSMAtgSSCKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSL 296
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 268370076 221 ALIVEPTSSVKLLLQQDTDLahkdiygftAEEYASFNGFTMYHHITANNENKKK 274
Cdd:PHA03095 297 MVRNNNGRAVRAALAKNPSA---------ETVAATLNTASVAGGDIPSDATRLC 341
PHA02878 PHA02878
ankyrin repeat protein; Provisional
51-250 4.62e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 71.83  E-value: 4.62e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076  51 LHKAATIGNEQKLKDYLERKkYNVNGRDKRSRTPLHLACAN------------------GYT-------------NIVSL 99
Cdd:PHA02878  41 LHQAVEARNLDVVKSLLTRG-HNVNQPDHRDLTPLHIICKEpnklgmkemirsinkcsvFYTlvaikdafnnrnvEIFKI 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076 100 LIENQCKiNVQDSENRTPLIKQAVECQQESCATVLLLHGADPNLVDVYS-NTALHYAVCGQNISLANKLLQYKANLEAKN 178
Cdd:PHA02878 120 ILTNRYK-NIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPD 198
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 268370076 179 KDGHTPLLLAVAENNENMVKFLLKKGADVNASDKNHRTAIMIAL-IVEPTSSVKLLLQQDTDL-AHKDIYGFTA 250
Cdd:PHA02878 199 KTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVgYCKDYDILKLLLEHGVDVnAKSYILGLTA 272
PHA02875 PHA02875
ankyrin repeat protein; Provisional
51-251 2.19e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 69.63  E-value: 2.19e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076  51 LHKAATIGNEQKLKDYLERKKYNVNGRDKRSRTPLHLACANGYTNIVSLLIENQCKINVQDSENRTPLiKQAVECQQESC 130
Cdd:PHA02875  72 LHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPL-HLAVMMGDIKG 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076 131 ATVLLLHGADPNLVDVYSNTALHYAVCGQNISLANKLLQYKANLEAKNKDGHTPLLLAVAENNE-NMVKFLLKKGADVNa 209
Cdd:PHA02875 151 IELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKiDIVRLFIKRGADCN- 229
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 268370076 210 sdknhrtaIMIALIVEPTSSVKLLLQQDTDLAHKDIYGFTAE 251
Cdd:PHA02875 230 --------IMFMIEGEECTILDMICNMCTNLESEAIDALIAD 263
PHA02876 PHA02876
ankyrin repeat protein; Provisional
72-257 9.10e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 68.17  E-value: 9.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076  72 YNVNGRDKRSRTPLHLAC-ANGYTNIVSLLIENQCKINVQDSENRTPLIKQAVECQQESCATVLLLHGADPNLVDVYSNT 150
Cdd:PHA02876 264 FSVNSIDDCKNTPLHHASqAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYDTENIRTLIMLGADVNAADRLYIT 343
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076 151 ALHYA-VCGQNISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKKGADVNASDKNHRTAIMIALI-VEPTS 228
Cdd:PHA02876 344 PLHQAsTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCgTNPYM 423
                        170       180
                 ....*....|....*....|....*....
gi 268370076 229 SVKLLLQQDTDLAHKDIYGFTAEEYASFN 257
Cdd:PHA02876 424 SVKTLIDRGANVNSKNKDLSTPLHYACKK 452
PHA03100 PHA03100
ankyrin repeat protein; Provisional
94-257 1.32e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 67.38  E-value: 1.32e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076  94 TNIVSLLIENQCKINVQDSENRTPLIKQAVECQQESCATVLLLHGADPNLVDVYSNTALHYAVCGQNISLANK-----LL 168
Cdd:PHA03100  14 KVKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLTDVKeivklLL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076 169 QYKANLEAKNKDGHTPLLLAVAE--NNENMVKFLLKKGADVNASDKNHRTAIMIALI------------------VEPTS 228
Cdd:PHA03100  94 EYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLEsnkidlkilkllidkgvdINAKN 173
                        170       180
                 ....*....|....*....|....*....
gi 268370076 229 SVKLLLQQDTDLAHKDIYGFTAEEYASFN 257
Cdd:PHA03100 174 RVNYLLSYGVPINIKDVYGFTPLHYAVYN 202
PHA02878 PHA02878
ankyrin repeat protein; Provisional
94-249 1.76e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 66.83  E-value: 1.76e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076  94 TNIVSLLIENQCKINVQDSENRTPLIKQAVECQQESCATVLLLHGADPNLVDVYSNTALHYAVCGQNISLANKLLQYKAN 173
Cdd:PHA02878 147 AEITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS 226
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 268370076 174 LEAKNKDGHTPLLLAVAE-NNENMVKFLLKKGADVNA-SDKNHRTAIMIALIVEptSSVKLLLQQDTDLAHKDIYGFT 249
Cdd:PHA02878 227 TDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAkSYILGLTALHSSIKSE--RKLKLLLEYGADINSLNSYKLT 302
PHA02878 PHA02878
ankyrin repeat protein; Provisional
39-222 1.54e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 64.13  E-value: 1.54e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076  39 GGYHLRDKHLKKLHKAATIgnEQKLKDYLERKKYNVNGRDKRS-RTPLHLACANGYTNIVSLLIENQCKINVQDSENRTP 117
Cdd:PHA02878 127 NIQTIDLVYIDKKSKDDII--EAEITKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSP 204
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076 118 LIKqAVECQQESCATVLLLHGADPNLVDVYSNTALHYAVCG-QNISLANKLLQYKANLEAKNK-DGHTPLLLAVaeNNEN 195
Cdd:PHA02878 205 LHH-AVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYiLGLTALHSSI--KSER 281
                        170       180
                 ....*....|....*....|....*..
gi 268370076 196 MVKFLLKKGADVNASDKNHRTAIMIAL 222
Cdd:PHA02878 282 KLKLLLEYGADINSLNSYKLTPLSSAV 308
PHA02878 PHA02878
ankyrin repeat protein; Provisional
35-189 1.58e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 64.13  E-value: 1.58e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076  35 LSIGGGYHLRDKHLKK--LHKAATiGNEQKLKDYLERKKYNVNGRDKRSRTPLHLACANGYTNIVSLLIENQCKINVQDS 112
Cdd:PHA02878 154 LSYGADINMKDRHKGNtaLHYATE-NKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDK 232
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 268370076 113 ENRTPLIKQAVECQQESCATVLLLHGADPNLVDVYSN-TALHYAVCGQNISlaNKLLQYKANLEAKNKDGHTPLLLAV 189
Cdd:PHA02878 233 CGNTPLHISVGYCKDYDILKLLLEHGVDVNAKSYILGlTALHSSIKSERKL--KLLLEYGADINSLNSYKLTPLSSAV 308
PHA02875 PHA02875
ankyrin repeat protein; Provisional
73-239 4.78e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 62.70  E-value: 4.78e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076  73 NVNGRDKRSrtPLHLACANGYTNIVSLLIENQCKIN-VQDSENRTPLiKQAVECQQESCATVLLLHGADPNLVDVYSNTA 151
Cdd:PHA02875  62 DVKYPDIES--ELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPL-HLATILKKLDIMKLLIARGADPDIPNTDKFSP 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076 152 LHYAVCGQNISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKKGADVNASDKNHRTAIM-IALIVEPTSSV 230
Cdd:PHA02875 139 LHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALcYAIENNKIDIV 218

                 ....*....
gi 268370076 231 KLLLQQDTD 239
Cdd:PHA02875 219 RLFIKRGAD 227
PHA03095 PHA03095
ankyrin-like protein; Provisional
62-203 5.98e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 62.35  E-value: 5.98e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076  62 KLKDYLERKKYNVNGRDKRSRTPLHLACAN--GYTNIVSLLIENQCKINVQDSENRTPLIKQAVECqqeSCATV----LL 135
Cdd:PHA03095 168 ELLRLLIDAGADVYAVDDRFRSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSMATGS---SCKRSlvlpLL 244
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 268370076 136 LHGADPNLVDVYSNTALHYAVCGQNISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKK 203
Cdd:PHA03095 245 IAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAK 312
PHA02874 PHA02874
ankyrin repeat protein; Provisional
83-249 8.71e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 61.90  E-value: 8.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076  83 TPLHLACANGYTNIVSLLIENQCKINVQDSENRTPLIKQ----------------------AVECQQESCATVLLLHGAD 140
Cdd:PHA02874  37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAikigahdiikllidngvdtsilPIPCIEKDMIKTILDCGID 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076 141 PNLVDVYSNTALHYAVCGQNISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKKGADVNASDKNHRTAIMI 220
Cdd:PHA02874 117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196
                        170       180
                 ....*....|....*....|....*....
gi 268370076 221 ALIVEPTSSVKLLLQQDTDLAHKDIYGFT 249
Cdd:PHA02874 197 AAEYGDYACIKLLIDHGNHIMNKCKNGFT 225
PHA02875 PHA02875
ankyrin repeat protein; Provisional
88-254 8.64e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 55.77  E-value: 8.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076  88 ACANGYTNIVSLLIENQCKINVQDSENRTPlIKQAVECQQESCATVLLLHGADPNLVDVYSNTALHYAVCGQNISLANKL 167
Cdd:PHA02875   9 AILFGELDIARRLLDIGINPNFEIYDGISP-IKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEEL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076 168 LQYKANL-EAKNKDGHTPLLLAVAENNENMVKFLLKKGADVNASDKNHRTAIMIALIVEPTSSVKLLLQQDTDLAHKDIY 246
Cdd:PHA02875  88 LDLGKFAdDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCC 167

                 ....*...
gi 268370076 247 GFTAEEYA 254
Cdd:PHA02875 168 GCTPLIIA 175
PHA02874 PHA02874
ankyrin repeat protein; Provisional
35-222 7.67e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.04  E-value: 7.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076  35 LSIGGGYHLRDKHLKK-LHKAATIGNEQKLKDYLERKKyNVNGRDKRSRTPLHLACANGYTNIVSLLIENQCKINVQDSE 113
Cdd:PHA02874 111 LDCGIDVNIKDAELKTfLHYAIKKGDLESIKMLFEYGA-DVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNN 189
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076 114 NRTPLiKQAVECQQESCATVLLLHGADPNLVDVYSNTALHYAVCgQNISlANKLLQYKANLEAKNKDGHTPLLLAVAEN- 192
Cdd:PHA02874 190 GESPL-HNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII-HNRS-AIELLINNASINDQDIDGSTPLHHAINPPc 266
                        170       180       190
                 ....*....|....*....|....*....|
gi 268370076 193 NENMVKFLLKKGADVNASDKNHRTAIMIAL 222
Cdd:PHA02874 267 DIDIIDILLYHKADISIKDNKGENPIDTAF 296
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
131-202 8.66e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.98  E-value: 8.66e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 268370076 131 ATVLLLHGADPNLVDVYSNTALHYAVCGQNISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLK 202
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
Ank_4 pfam13637
Ankyrin repeats (many copies);
181-234 1.09e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.65  E-value: 1.09e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 268370076  181 GHTPLLLAVAENNENMVKFLLKKGADVNASDKNHRTAIMIALIVEPTSSVKLLL 234
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
66-118 1.83e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.96  E-value: 1.83e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 268370076   66 YLERKKYNVNGRDKRSRTPLHLACANGYTNIVSLLIENQCKINVQDSENRTPL 118
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PHA02874 PHA02874
ankyrin repeat protein; Provisional
95-254 6.70e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 49.96  E-value: 6.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076  95 NIVSLLIENQCKINVQDSENRTpLIKQAVECQQESCATVLLLHGADPNLVDVYSNTALHYAVCGQNISLANKLLQYKANL 174
Cdd:PHA02874 105 DMIKTILDCGIDVNIKDAELKT-FLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYA 183
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076 175 EAKNKDGHTPLLLAVAENNENMVKFLLKKGADVNASDKNHRTAIMIAlIVEPTSSVKLLLQQDTdLAHKDIYGFTAEEYA 254
Cdd:PHA02874 184 NVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA-IIHNRSAIELLINNAS-INDQDIDGSTPLHHA 261
Ank_4 pfam13637
Ankyrin repeats (many copies);
149-201 1.48e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 1.48e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 268370076  149 NTALHYAVCGQNISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLL 201
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
131-241 1.59e-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: 48.86  E-value: 1.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076 131 ATVLLLHGAdPNLV------DVYSN-TALHYAVCGQNISLANKLLQYKANLEA---------KNKD-----GHTPLLLAV 189
Cdd:cd22192   66 AAVVLMEAA-PELVnepmtsDLYQGeTALHIAVVNQNLNLVRELIARGADVVSpratgtffrPGPKnliyyGEHPLSFAA 144
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 268370076 190 AENNENMVKFLLKKGADVNASDKNHRTAIMIaliveptssvkLLLQQDTDLA 241
Cdd:cd22192  145 CVGNEEIVRLLIEHGADIRAQDSLGNTVLHI-----------LVLQPNKTFA 185
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
114-207 2.03e-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: 48.86  E-value: 2.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076 114 NRTPLIKQAVECQQESCATVLLLHGADPNLVDVYSNTALHYAVCGQNISLANKLLQYKANL--EAKNKD---GHTPLLLA 188
Cdd:cd22192   17 SESPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELvnEPMTSDlyqGETALHIA 96
                         90
                 ....*....|....*....
gi 268370076 189 VAENNENMVKFLLKKGADV 207
Cdd:cd22192   97 VVNQNLNLVRELIARGADV 115
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
83-203 2.94e-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: 2.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076  83 TPLHLACANGYTNIVSLLIENQCkiNVQD--------SENRTPLI-------KQAVECQQESCATVLLLHGADPNLVDVY 147
Cdd:cd22192   91 TALHIAVVNQNLNLVRELIARGA--DVVSpratgtffRPGPKNLIyygehplSFAACVGNEEIVRLLIEHGADIRAQDSL 168
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 268370076 148 SNTALHYAVCGQNISLA----NKLLQYKANLEA------KNKDGHTPLLLAVAENNENMVKFLLKK 203
Cdd:cd22192  169 GNTVLHILVLQPNKTFAcqmyDLILSYDKEDDLqpldlvPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
180-212 3.61e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 42.66  E-value: 3.61e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 268370076  180 DGHTPLLLAVAE-NNENMVKFLLKKGADVNASDK 212
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
Ank_4 pfam13637
Ankyrin repeats (many copies);
51-101 6.25e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.65  E-value: 6.25e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 268370076   51 LHKAATIGNEQKLKDYLErKKYNVNGRDKRSRTPLHLACANGYTNIVSLLI 101
Cdd:pfam13637   5 LHAAAASGHLELLRLLLE-KGADINAVDGNGETALHFAASNGNVEVLKLLL 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
49-209 6.31e-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: 47.38  E-value: 6.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076   49 KKLHKAATIGNEQKLKDYL-ERKKYNVNGRDKRSRTPL-HLACANGYTNIVSLLIENQCKINVQDSenrtplikqavecq 126
Cdd:TIGR00870  19 KAFLPAAERGDLASVYRDLeEPKKLNINCPDRLGRSALfVAAIENENLELTELLLNLSCRGAVGDT-------------- 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076  127 qescatvlLLHGADPNLVDVYSNTALH---YAVCGQNISLANKllQYKANLEAknkdGHTPLLLAVAENNENMVKFLLKK 203
Cdd:TIGR00870  85 --------LLHAISLEYVDAVEAILLHllaAFRKSGPLELAND--QYTSEFTP----GITALHLAAHRQNYEIVKLLLER 150

                  ....*.
gi 268370076  204 GADVNA 209
Cdd:TIGR00870 151 GASVPA 156
PHA02798 PHA02798
ankyrin-like protein; Provisional
73-270 6.60e-06

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 47.14  E-value: 6.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076  73 NVNGRDKRSRTPLHLACAN-----GYTNIVSLLIENQCKINVQDSENRTPLIKQAVECQQESCATVLLL--HGADPNLVD 145
Cdd:PHA02798  63 NVNGLDNEYSTPLCTILSNikdykHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLFMieNGADTTLLD 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076 146 VYSNTALHYAV---CGQNISLANKLLQYKANLEA-KNKDGHTPLLLAVAEN----NENMVKFLLKKGADVNASDKNHRTA 217
Cdd:PHA02798 143 KDGFTMLQVYLqsnHHIDIEIIKLLLEKGVDINThNNKEKYDTLHCYFKYNidriDADILKLFVDNGFIINKENKSHKKK 222
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 268370076 218 IMIALIVeptssvkllLQQDTDLAHKDIYGF-----TAEEYASFNGFTMYHHITANNE 270
Cdd:PHA02798 223 FMEYLNS---------LLYDNKRFKKNILDFifsyiDINQVDELGFNPLYYSVSHNNR 271
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
75-137 7.97e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.82  E-value: 7.97e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 268370076  75 NGRDKRSRTPLHLACANGYTNIVSLLIENQCKINVQDSENRTPLiKQAVECQQESCATVLLLH 137
Cdd:PTZ00322 109 NCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPL-ELAEENGFREVVQLLSRH 170
Ank_5 pfam13857
Ankyrin repeats (many copies);
134-188 1.45e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.56  E-value: 1.45e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 268370076  134 LLLHG-ADPNLVDVYSNTALHYAVCGQNISLANKLLQYKANLEAKNKDGHTPLLLA 188
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
180-209 1.64e-05

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: 41.03  E-value: 1.64e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 268370076   180 DGHTPLLLAVAENNENMVKFLLKKGADVNA 209
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
114-168 4.71e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.34  E-value: 4.71e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 268370076  114 NRTPLIKQAVECQQESCATvLLLHGADPNLVDVYSNTALHYAVCGQNISLANKLL 168
Cdd:pfam13637   1 ELTALHAAAASGHLELLRL-LLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
180-209 6.63e-05

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.16  E-value: 6.63e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 268370076  180 DGHTPLLLAVAENNENMVKFLLKKGADVNA 209
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
57-242 7.88e-05

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 43.72  E-value: 7.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076  57 IGNEQKLKDYLERKKYNvngRDKRSRTPLHLACAN---GYTNIVSLLIENQckinvQDSENRTPLIKQAVECQqescatv 133
Cdd:cd21882    5 LGLLECLRWYLTDSAYQ---RGATGKTCLHKAALNlndGVNEAIMLLLEAA-----PDSGNPKELVNAPCTDE------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076 134 lLLHGadpnlvdvysNTALHYAVCGQNISLANKLLQYKANLEAK------NKDGHT-------PLLLAVAENNENMVKFL 200
Cdd:cd21882   70 -FYQG----------QTALHIAIENRNLNLVRLLVENGADVSARatgrffRKSPGNlfyfgelPLSLAACTNQEEIVRLL 138
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 268370076 201 LKKGAD---VNASDKNHRTaIMIALIVEPTSSVK----------LLLQQDTDLAH 242
Cdd:cd21882  139 LENGAQpaaLEAQDSLGNT-VLHALVLQADNTPEnsafvcqmynLLLSYGAHLDP 192
Ank_4 pfam13637
Ankyrin repeats (many copies);
82-135 1.03e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.18  E-value: 1.03e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 268370076   82 RTPLHLACANGYTNIVSLLIENQCKINVQDSENRTPLIKqAVECQQESCATVLL 135
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHF-AASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
154-271 1.34e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 42.73  E-value: 1.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076 154 YAVCGQNISLANKLLQYKANLEA----KNKDGHTPLLLAVAENNENMVKFLLKKGADVNASDKNHRTAIMIALIVEPTSS 229
Cdd:PHA03100   4 YIVLTKSRIIKVKNIKYIIMEDDlndySYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLT 83
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 268370076 230 -----VKLLLQQDTDLAHKDIYGFTAEEYA---SFNGFTMYHHITANNEN 271
Cdd:PHA03100  84 dvkeiVKLLLEYGANVNAPDNNGITPLLYAiskKSNSYSIVEYLLDNGAN 133
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
82-109 4.46e-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: 36.85  E-value: 4.46e-04
                          10        20
                  ....*....|....*....|....*...
gi 268370076   82 RTPLHLACANGYTNIVSLLIENQCKINV 109
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
82-111 5.41e-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: 5.41e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 268370076   82 RTPLHLACA-NGYTNIVSLLIENQCKINVQD 111
Cdd:pfam00023   3 NTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
PHA02736 PHA02736
Viral ankyrin protein; Provisional
77-205 5.60e-04

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 39.47  E-value: 5.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076  77 RDKRSRTPLHLACANGytNIVSLLIENqckiNVQDSENR---TPLIKQAVEC-----------QQESCaTVLLLHGADPN 142
Cdd:PHA02736  13 PDIEGENILHYLCRNG--GVTDLLAFK----NAISDENRylvLEYNRHGKQCvhivsnpdkadPQEKL-KLLMEWGADIN 85
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 268370076 143 LVD-VYSNTALHYAVCGQNISLANKLL-QYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKKGA 205
Cdd:PHA02736  86 GKErVFGNTPLHIAVYTQNYELATWLCnQPGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGA 150
Ank_5 pfam13857
Ankyrin repeats (many copies);
167-221 5.74e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.33  E-value: 5.74e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 268370076  167 LLQYK-ANLEAKNKDGHTPLLLAVAENNENMVKFLLKKGADVNASDKNHRTAIMIA 221
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
82-109 1.19e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.64  E-value: 1.19e-03
                           10        20
                   ....*....|....*....|....*...
gi 268370076    82 RTPLHLACANGYTNIVSLLIENQCKINV 109
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02884 PHA02884
ankyrin repeat protein; Provisional
93-196 3.05e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 38.43  E-value: 3.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076  93 YTNIVSLLIENQCKINVQ--DSENR--TPLIkQAVECQQESCATVLLLHGADpnlVDVYSN----TALHYAVCGQNISLA 164
Cdd:PHA02884  45 YTDIIDAILKLGADPEAPfpLSENSktNPLI-YAIDCDNDDAAKLLIRYGAD---VNRYAEeakiTPLYISVLHGCLKCL 120
                         90       100       110
                 ....*....|....*....|....*....|..
gi 268370076 165 NKLLQYKANLEAKNKDGHTPLLLAVAENNENM 196
Cdd:PHA02884 121 EILLSYGADINIQTNDMVTPIELALMICNNFL 152
PHA02946 PHA02946
ankyin-like protein; Provisional
108-212 3.81e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 38.50  E-value: 3.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076 108 NVQDSENRTPLiKQAVECQQESCATVLLLHGADPNLVDVYSNTALHY--AVCGQNISLANKLLQYKANL-EAKNKDGHTP 184
Cdd:PHA02946  66 NETDDDGNYPL-HIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYlsGTDDEVIERINLLVQYGAKInNSVDEEGCGP 144
                         90       100
                 ....*....|....*....|....*...
gi 268370076 185 lLLAVAENNENMVKFLLKKGADVNASDK 212
Cdd:PHA02946 145 -LLACTDPSERVFKKIMSIGFEARIVDK 171
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
140-221 5.39e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 37.96  E-value: 5.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076 140 DPNLVDVYSNTALHYAVCGQNISlANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKKGADVNASDKNHRTAIM 219
Cdd:PTZ00322  75 DPVVAHMLTVELCQLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLE 153

                 ..
gi 268370076 220 IA 221
Cdd:PTZ00322 154 LA 155
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
160-223 8.32e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 37.54  E-value: 8.32e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 268370076 160 NISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKKGADVNASDKNHRTAIMIALI 223
Cdd:PLN03192 537 NAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAIS 600
PHA02798 PHA02798
ankyrin-like protein; Provisional
94-249 9.07e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 37.12  E-value: 9.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076  94 TNIVSLLIENQCKINVQDSENRTPLikqavecqqescATVLllhgadPNLVDVYSntalhyavcgqNISLANKLLQYKAN 173
Cdd:PHA02798  51 TDIVKLFINLGANVNGLDNEYSTPL------------CTIL------SNIKDYKH-----------MLDIVKILIENGAD 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268370076 174 LEAKNKDGHTPLLLAVAE---NNENMVKFLLKKGADVNASDKNHRTAIMIALIVE---PTSSVKLLLQQDTDL-AHKDIY 246
Cdd:PHA02798 102 INKKNSDGETPLYCLLSNgyiNNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNhhiDIEIIKLLLEKGVDInTHNNKE 181

                 ...
gi 268370076 247 GFT 249
Cdd:PHA02798 182 KYD 184
 
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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