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Conserved domains on  [gi|1034644475|ref|XP_016864807|]
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ankyrin repeat domain-containing protein 31 isoform X5 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1206-1345 5.60e-38

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 145.10  E-value: 5.60e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475 1206 INKRNARGESQLHLAVRRGNLPLVKALIESGADVNLNDNAGWTPLHEASNEGSIDIIVELLKAGAKVNCENIDGILPLHD 1285
Cdd:COG0666    113 VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHL 192

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034644475 1286 AVANNHLKAAEILLQNGANPNQKDQKQKSALDEA----DDEKMKELLRSYGAIETVNRDESDAI 1345
Cdd:COG0666    193 AAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAaengNLEIVKLLLEAGADLNAKDKDGLTAL 256
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
483-612 6.27e-28

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 115.82  E-value: 6.27e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475  483 INRRNIFGENLVYKAALHDDADLVHHCIKKGGNVNQPSYAGWTALHEASVGGFYRTASELLKGGADVNIKGLYQITPLHD 562
Cdd:COG0666    113 VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHL 192

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1034644475  563 AVMNGHYKVAELLLLNGADPLFRNDDGKCALDEAKDLCMKRLLERYIPKH 612
Cdd:COG0666    193 AAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242
RAMA super family cl16759
Restriction Enzyme Adenine Methylase Associated; An alpha+beta fold domain associated with ...
 1739-1778 4.36e-04

Restriction Enzyme Adenine Methylase Associated; An alpha+beta fold domain associated with restriction enzymes across prokaryotes and fused to JAB deubiquitinases, and chromatin proteins in a wide range of eukaryotes. The domain is predicted to function as a modified-DNA reader domain.


The actual alignment was detected with superfamily member pfam18755:

Pssm-ID: 473011  Cd Length: 108  Bit Score: 41.53  E-value: 4.36e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1034644475 1739 TIKKALNYSTAPKKKCIQIKDLILLGRINPGNNIL--EFKTQ 1778
Cdd:pfam18755    3 SESAPSGGSSRRTGRRVTLQDLLEAGLLQPGEGLLsiEYKGQ 44
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1206-1345 5.60e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 145.10  E-value: 5.60e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475 1206 INKRNARGESQLHLAVRRGNLPLVKALIESGADVNLNDNAGWTPLHEASNEGSIDIIVELLKAGAKVNCENIDGILPLHD 1285
Cdd:COG0666    113 VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHL 192

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034644475 1286 AVANNHLKAAEILLQNGANPNQKDQKQKSALDEA----DDEKMKELLRSYGAIETVNRDESDAI 1345
Cdd:COG0666    193 AAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAaengNLEIVKLLLEAGADLNAKDKDGLTAL 256
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
483-612 6.27e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 115.82  E-value: 6.27e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475  483 INRRNIFGENLVYKAALHDDADLVHHCIKKGGNVNQPSYAGWTALHEASVGGFYRTASELLKGGADVNIKGLYQITPLHD 562
Cdd:COG0666    113 VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHL 192

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1034644475  563 AVMNGHYKVAELLLLNGADPLFRNDDGKCALDEAKDLCMKRLLERYIPKH 612
Cdd:COG0666    193 AAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1217-1309 5.53e-25

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 100.58  E-value: 5.53e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475 1217 LHLAVRRGNLPLVKALIESGADVNLNDNAGWTPLHEASNEGSIDiIVELLKAGAKVNCENiDGILPLHDAVANNHLKAAE 1296
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLE-IVKLLLEHADVNLKD-NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 1034644475 1297 ILLQNGANPNQKD 1309
Cdd:pfam12796   79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
497-586 2.38e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 73.23  E-value: 2.38e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475  497 AALHDDADLVHHCIKKGGNVNQPSYAGWTALHEASVGGFYRTASELLKGgADVNIKGlYQITPLHDAVMNGHYKVAELLL 576
Cdd:pfam12796    4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLL 81

                           90
                   ....*....|
gi 1034644475  577 LNGADPLFRN 586
Cdd:pfam12796   82 EKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 1193-1440 1.59e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 75.00  E-value: 1.59e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475 1193 LKTTCNLGMKagrINKRNARGESQLHLAVRRGNLPLVKALIESGADVNLNDNAGWTPLHEASNEGSIDIIVELLKAGAKV 1272
Cdd:PHA02874   107 IKTILDCGID---VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYA 183

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475 1273 NCENIDGILPLHDAVANNHLKAAEILLQNGANPNQKDQKQKSALDEAddekmkeLLRSYGAIETV--NRDESDAIVNEKI 1350
Cdd:PHA02874   184 NVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA-------IIHNRSAIELLinNASINDQDIDGST 256

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475 1351 PavrskrhkqcfcddgktidsssLSHQERSRESLSVHQTLSAILQDIEEKQEyllefEIRNPED-AEQYIEKMLKIKKIM 1429
Cdd:PHA02874   257 P----------------------LHHAINPPCDIDIIDILLYHKADISIKDN-----KGENPIDtAFKYINKDPVIKDII 309

                          250
                   ....*....|.
gi 1034644475 1430 DNVLAKQKAER 1440
Cdd:PHA02874   310 ANAVLIKEADK 320
PHA03095 PHA03095
ankyrin-like protein; Provisional
 498-594 1.34e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 59.65  E-value: 1.34e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475  498 ALHDDADLVHHCIKKGGNVNQPSYAGWTALHeasvggFYRTASE-------LLKGGADVNIKGLYQITPLHD--AVMNGH 568
Cdd:PHA03095    58 SSEKVKDIVRLLLEAGADVNAPERCGFTPLH------LYLYNATtldviklLIKAGADVNAKDKVGRTPLHVylSGFNIN 131

                           90       100
                   ....*....|....*....|....*.
gi 1034644475  569 YKVAELLLLNGADPLFRNDDGKCALD 594
Cdd:PHA03095   132 PKVIRLLLRKGADVNALDLYGMTPLA 157
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 1209-1309 1.43e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 46.93  E-value: 1.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475 1209 RNARGESQLHLAVRRGNLPLVKALIESGAD-VNLNDN----AGWTPLHEASNEGSIDIIVELLKAGAKVNC--------- 1274
Cdd:cd22192     47 RGALGETALHVAALYDNLEAAVVLMEAAPElVNEPMTsdlyQGETALHIAVVNQNLNLVRELIARGADVVSpratgtffr 126

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1034644475 1275 ENIDGIL-----PLHDAVANNHLKAAEILLQNGANPNQKD 1309
Cdd:cd22192    127 PGPKNLIyygehPLSFAACVGNEEIVRLLIEHGADIRAQD 166
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 1246-1274 2.34e-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: 39.88  E-value: 2.34e-04
                            10        20
                    ....*....|....*....|....*....
gi 1034644475  1246 GWTPLHEASNEGSIDIIVELLKAGAKVNC 1274
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
RAMA pfam18755
Restriction Enzyme Adenine Methylase Associated; An alpha+beta fold domain associated with ...
 1739-1778 4.36e-04

Restriction Enzyme Adenine Methylase Associated; An alpha+beta fold domain associated with restriction enzymes across prokaryotes and fused to JAB deubiquitinases, and chromatin proteins in a wide range of eukaryotes. The domain is predicted to function as a modified-DNA reader domain.


Pssm-ID: 465856  Cd Length: 108  Bit Score: 41.53  E-value: 4.36e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1034644475 1739 TIKKALNYSTAPKKKCIQIKDLILLGRINPGNNIL--EFKTQ 1778
Cdd:pfam18755    3 SESAPSGGSSRRTGRRVTLQDLLEAGLLQPGEGLLsiEYKGQ 44
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 555-582 6.07e-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: 38.72  E-value: 6.07e-04
                            10        20
                    ....*....|....*....|....*...
gi 1034644475   555 YQITPLHDAVMNGHYKVAELLLLNGADP 582
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 486-588 3.22e-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: 42.31  E-value: 3.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475  486 RNIFGENLVYKAALHDDADLVHHCIKKG-GNVNQPS----YAGWTALHEASVGGFYRTASELLKGGADV----------- 549
Cdd:cd22192     47 RGALGETALHVAALYDNLEAAVVLMEAApELVNEPMtsdlYQGETALHIAVVNQNLNLVRELIARGADVvspratgtffr 126

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1034644475  550 -NIKGL--YQITPLHDAVMNGHYKVAELLLLNGADPlfRNDD 588
Cdd:cd22192    127 pGPKNLiyYGEHPLSFAACVGNEEIVRLLIEHGADI--RAQD 166
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1206-1345 5.60e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 145.10  E-value: 5.60e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475 1206 INKRNARGESQLHLAVRRGNLPLVKALIESGADVNLNDNAGWTPLHEASNEGSIDIIVELLKAGAKVNCENIDGILPLHD 1285
Cdd:COG0666    113 VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHL 192

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034644475 1286 AVANNHLKAAEILLQNGANPNQKDQKQKSALDEA----DDEKMKELLRSYGAIETVNRDESDAI 1345
Cdd:COG0666    193 AAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAaengNLEIVKLLLEAGADLNAKDKDGLTAL 256
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1202-1345 3.17e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 140.09  E-value: 3.17e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475 1202 KAGRINKRNARGESQLHLAVRRGNLPLVKALIESGADVNLNDNAGWTPLHEASNEGSIDIIVELLKAGAKVNCENIDGIL 1281
Cdd:COG0666     76 AGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNT 155

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034644475 1282 PLHDAVANNHLKAAEILLQNGANPNQKDQKQKSALDEA---DDEKMKELLRSYGA-IETVNRDESDAI 1345
Cdd:COG0666    156 PLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAaenGHLEIVKLLLEAGAdVNAKDNDGKTAL 223
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1206-1329 1.81e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 120.44  E-value: 1.81e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475 1206 INKRNARGESQLHLAVRRGNLPLVKALIESGADVNLNDNAGWTPLHEASNEGSIDIIVELLKAGAKVNCENIDGILPLHD 1285
Cdd:COG0666    146 VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDL 225

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1034644475 1286 AVANNHLKAAEILLQNGANPNQKDQKQKSALDEADDEKMKELLR 1329
Cdd:COG0666    226 AAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVK 269
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
483-612 6.27e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 115.82  E-value: 6.27e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475  483 INRRNIFGENLVYKAALHDDADLVHHCIKKGGNVNQPSYAGWTALHEASVGGFYRTASELLKGGADVNIKGLYQITPLHD 562
Cdd:COG0666    113 VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHL 192

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1034644475  563 AVMNGHYKVAELLLLNGADPLFRNDDGKCALDEAKDLCMKRLLERYIPKH 612
Cdd:COG0666    193 AAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
411-596 8.71e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 109.66  E-value: 8.71e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475  411 EKILPKILGCEDLTNNNSSAQNFRMQDPALMIDGKEKNMHSARFKNGKQIRKNEQFSGKKEKMKVNKISLHSINRRNIFG 490
Cdd:COG0666      8 LLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGG 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475  491 ENLVYKAALHDDADLVHHCIKKGGNVNQPSYAGWTALHEASVGGFYRTASELLKGGADVNIKGLYQITPLHDAVMNGHYK 570
Cdd:COG0666     88 NTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLE 167

                          170       180
                   ....*....|....*....|....*.
gi 1034644475  571 VAELLLLNGADPLFRNDDGKCALDEA 596
Cdd:COG0666    168 IVKLLLEAGADVNARDNDGETPLHLA 193
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1217-1309 5.53e-25

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 100.58  E-value: 5.53e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475 1217 LHLAVRRGNLPLVKALIESGADVNLNDNAGWTPLHEASNEGSIDiIVELLKAGAKVNCENiDGILPLHDAVANNHLKAAE 1296
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLE-IVKLLLEHADVNLKD-NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 1034644475 1297 ILLQNGANPNQKD 1309
Cdd:pfam12796   79 LLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1199-1354 3.88e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 104.65  E-value: 3.88e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475 1199 LGMKAGRINKRNARGESQLHLAVRRGNLPLVKALIESGADVNLNDNAGWTPLHEASNEGSIDIIVELLKAGAKVNCENID 1278
Cdd:COG0666     40 LLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKD 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475 1279 GILPLHDAVANNHLKAAEILLQNGANPNQKDQKQKSALDEA---DDEKMKELLRSYGA-IETVNRDES----DAIVNEKI 1350
Cdd:COG0666    120 GETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAaanGNLEIVKLLLEAGAdVNARDNDGEtplhLAAENGHL 199


                   ....
gi 1034644475 1351 PAVR 1354
Cdd:COG0666    200 EIVK 203
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1206-1316 1.70e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 93.87  E-value: 1.70e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475 1206 INKRNARGESQLHLAVRRGNLPLVKALIESGADVNLNDNAGWTPLHEASNEGSIDIIVELLKAGAKVNCENIDGILPLHD 1285
Cdd:COG0666    179 VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLL 258

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1034644475 1286 AVANNHLKAAEILLQNGANPNQKDQKQKSAL 1316
Cdd:COG0666    259 AAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
483-614 2.20e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 93.48  E-value: 2.20e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475  483 INRRNIFGENLVYKAALHDDADLVHHCIKKGGNVNQPSYAGWTALHEASVGGFYRTASELLKGGADVNIKGLYQITPLHD 562
Cdd:COG0666    146 VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDL 225

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1034644475  563 AVMNGHYKVAELLLLNGADPLFRNDDGKCALDEAKDLCMKRLLERYIPKHQK 614
Cdd:COG0666    226 AAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLL 277
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
440-607 4.48e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 89.63  E-value: 4.48e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475  440 LMIDGKEKNMHSARFKNGKQIRKNEQFSGKKEKMKVNKISLHSINRRNIFGENLVYKAALHDDADLVHHCIKKGGNVNQP 519
Cdd:COG0666      4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475  520 SYAGWTALHEASVGGFYRTASELLKGGADVNIKGLYQITPLHDAVMNGHYKVAELLLLNGADPLFRNDDGKCALDEA--- 596
Cdd:COG0666     84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAaan 163

                          170
                   ....*....|..
gi 1034644475  597 KDL-CMKRLLER 607
Cdd:COG0666    164 GNLeIVKLLLEA 175
Ank_2 pfam12796
Ankyrin repeats (3 copies);
497-586 2.38e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 73.23  E-value: 2.38e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475  497 AALHDDADLVHHCIKKGGNVNQPSYAGWTALHEASVGGFYRTASELLKGgADVNIKGlYQITPLHDAVMNGHYKVAELLL 576
Cdd:pfam12796    4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLL 81

                           90
                   ....*....|
gi 1034644475  577 LNGADPLFRN 586
Cdd:pfam12796   82 EKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1198-1333 2.30e-14

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 75.76  E-value: 2.30e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475 1198 NLGMKAGRINKRNARGESQLHLAVRRGNLPLVKALIESGADVNLNDNAGWTPLHEASNEGSIDIIVELLKAGAKVNCENI 1277
Cdd:COG0666      6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034644475 1278 DGILPLHDAVANNHLKAAEILLQNGANPNQKDQKQKSALDEA---DDEKMKELLRSYGA 1333
Cdd:COG0666     86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAaynGNLEIVKLLLEAGA 144
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 1193-1440 1.59e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 75.00  E-value: 1.59e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475 1193 LKTTCNLGMKagrINKRNARGESQLHLAVRRGNLPLVKALIESGADVNLNDNAGWTPLHEASNEGSIDIIVELLKAGAKV 1272
Cdd:PHA02874   107 IKTILDCGID---VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYA 183

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475 1273 NCENIDGILPLHDAVANNHLKAAEILLQNGANPNQKDQKQKSALDEAddekmkeLLRSYGAIETV--NRDESDAIVNEKI 1350
Cdd:PHA02874   184 NVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA-------IIHNRSAIELLinNASINDQDIDGST 256

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475 1351 PavrskrhkqcfcddgktidsssLSHQERSRESLSVHQTLSAILQDIEEKQEyllefEIRNPED-AEQYIEKMLKIKKIM 1429
Cdd:PHA02874   257 P----------------------LHHAINPPCDIDIIDILLYHKADISIKDN-----KGENPIDtAFKYINKDPVIKDII 309

                          250
                   ....*....|.
gi 1034644475 1430 DNVLAKQKAER 1440
Cdd:PHA02874   310 ANAVLIKEADK 320
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1206-1276 3.73e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.98  E-value: 3.73e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034644475 1206 INKRNARGESQLHLAVRRGNLPLVKALIESgADVNLNDNaGWTPLHEASNEGSIDIIVELLKAGAKVNCEN 1276
Cdd:pfam12796   23 ANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1206-1338 7.80e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 70.05  E-value: 7.80e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475 1206 INKRNARGESQLHLAVRRGNLPL---VKALIESGADVNLNDNAGWTPLH-EASNEGSIDIIVELLKAGAKVNCENIDGIL 1281
Cdd:PHA03095    40 VNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRT 119

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475 1282 PLHD--AVANNHLKAAEILLQNGANPNQKDQKQKSALDeaddekmkELLRSYGA-IETVN 1338
Cdd:PHA03095   120 PLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLA--------VLLKSRNAnVELLR 171
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
483-590 2.98e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 66.52  E-value: 2.98e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475  483 INRRNIFGENLVYKAALHDDADLVHHCIKKGGNVNQPSYAGWTALHEASVGGFYRTASELLKGGADVNIKGLYQITPLHD 562
Cdd:COG0666    179 VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLL 258

                           90       100
                   ....*....|....*....|....*...
gi 1034644475  563 AVMNGHYKVAELLLLNGADPLFRNDDGK 590
Cdd:COG0666    259 AAAAGAALIVKLLLLALLLLAAALLDLL 286
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
471-607 6.79e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 65.36  E-value: 6.79e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475  471 EKMKVNKISLHSINRRNIFGENLVYKAALHDDADLVHHCIKKGGNVNQPSYAGWTALHEASVGGFYRTASELLKGGADVN 550
Cdd:COG0666      2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034644475  551 IKGLYQITPLHDAVMNGHYKVAELLLLNGADPLFRNDDGKCALDEA---KDL-CMKRLLER 607
Cdd:COG0666     82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAaynGNLeIVKLLLEA 142
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1206-1310 1.04e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 66.23  E-value: 1.04e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475 1206 INKRNARGESQLHLAVR--RGNLPLVKALIESGADVN----------------LNDNAGWTPLHEASNEGSIDIIVELLK 1267
Cdd:PHA03100   134 VNIKNSDGENLLHLYLEsnKIDLKILKLLIDKGVDINaknrvnyllsygvpinIKDVYGFTPLHYAVYNNNPEFVKYLLD 213

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1034644475 1268 AGAKVNCENIDGILPLHDAVANNHLKAAEILLQNGANPNQKDQ 1310
Cdd:PHA03100   214 LGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 1159-1309 9.11e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 63.06  E-value: 9.11e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475 1159 NCEEIKEKTESEIHMPTNSQEHKTVQNFRKRQSFLKTTCNLGMKAGRINKRNARGESQLHLAVRRGNLPLVKALIESGAD 1238
Cdd:PHA02874   103 EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY 182

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034644475 1239 VNLNDNAGWTPLHEASNEGSIDIIVELLKAGAKVNCENIDGILPLHDAVANNhlKAAEILLQNGANPNQKD 1309
Cdd:PHA02874   183 ANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHN--RSAIELLINNASINDQD 251
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1217-1333 2.05e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 61.99  E-value: 2.05e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475 1217 LHLAVRRGNLPLVKALIESGADVNLNDNAGWTPLHEASNEGSI-----DIIVELLKAGAKVNCENIDGILPLHDAVAN-- 1289
Cdd:PHA03100    39 LYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKks 118

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1034644475 1290 NHLKAAEILLQNGANPNQKDQKQKSALDEA-----DDEKMKELLRSYGA 1333
Cdd:PHA03100   119 NSYSIVEYLLDNGANVNIKNSDGENLLHLYlesnkIDLKILKLLIDKGV 167
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 1206-1316 2.10e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 62.39  E-value: 2.10e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475 1206 INKRNARGESQLHLAVRRG-NLPLVKALIESGADVNLNDNAGWTPLHEASN-EGSIDIIVELLKAGAKVNCENIDGILPL 1283
Cdd:PHA02876   300 VNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPI 379

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1034644475 1284 HDAVANNHLKAAEILLQNGANPNQKDQKQKSAL 1316
Cdd:PHA02876   380 HYAAVRNNVVIINTLLDYGADIEALSQKIGTAL 412
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 1173-1345 2.15e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 62.58  E-value: 2.15e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475 1173 MPTNSQEHKTV-QNFRKRQSFLKttcnlGMKAGRI------NKRNARGESQLHLAVRRGNLPLVKALIESGADVNLNDNA 1245
Cdd:PLN03192   483 MQTRQEDNVVIlKNFLQHHKELH-----DLNVGDLlgdnggEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSK 557

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475 1246 GWTPLHEASNEGSIDIIVELLKAGAKVNCENIDGILPLHDAVANNHLKAAEILLQ--NGANPNQKDQKQKSALDEADDEK 1323
Cdd:PLN03192   558 GRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHfaSISDPHAAGDLLCTAAKRNDLTA 637

                          170       180
                   ....*....|....*....|..
gi 1034644475 1324 MKELLRSYGAIETVNRDESDAI 1345
Cdd:PLN03192   638 MKELLKQGLNVDSEDHQGATAL 659
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 1228-1319 2.50e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 61.90  E-value: 2.50e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475 1228 LVKALIESGADVNLNDNAGWTPLHEASNEGSIDIIVELLKAGAKVNCENIDGILPLHDAVANNHLKAAEILLQNGANPNQ 1307
Cdd:PHA02874   106 MIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANV 185

                           90
                   ....*....|..
gi 1034644475 1308 KDQKQKSALDEA 1319
Cdd:PHA02874   186 KDNNGESPLHNA 197
Ank_4 pfam13637
Ankyrin repeats (many copies);
1217-1266 2.62e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.59  E-value: 2.62e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1034644475 1217 LHLAVRRGNLPLVKALIESGADVNLNDNAGWTPLHEASNEGSIDIIVELL 1266
Cdd:pfam13637    5 LHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1198-1330 3.16e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 61.58  E-value: 3.16e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475 1198 NLGMKAG-RINKRNARGESQLHLAVRRGN-LPLVKALIESGADVNLNDNAGWTPLH-----EASNEGSIDIiveLLKAGA 1270
Cdd:PHA03095    67 RLLLEAGaDVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGADVNAKDKVGRTPLHvylsgFNINPKVIRL---LLRKGA 143

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034644475 1271 KVNCENIDGILPLHDAVANNHLKAA--EILLQNGANPNQKDQKQKSALD------EADDEKMKELLRS 1330
Cdd:PHA03095   144 DVNALDLYGMTPLAVLLKSRNANVEllRLLIDAGADVYAVDDRFRSLLHhhlqsfKPRARIVRELIRA 211
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 1199-1319 3.67e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 61.43  E-value: 3.67e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475 1199 LGMKAGRINKRNARGESQLHLAVRRGNLPLVKALIESGADVNLNDNAGWTPLHEASNE-GSIDIIVELLKAGAKVNCEN- 1276
Cdd:PHA02878   187 LLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSy 266

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1034644475 1277 IDGILPLHDAVANNhlKAAEILLQNGANPNQKDQKQKSALDEA 1319
Cdd:PHA02878   267 ILGLTALHSSIKSE--RKLKLLLEYGADINSLNSYKLTPLSSA 307
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 1228-1309 4.48e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 61.05  E-value: 4.48e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475 1228 LVKALIESGADVNLND-NAGWTPLHEASNEGSIDIIVELLKAGAKVNCENIDGILPLHDAVANNHLKAAEILLQNGANPN 1306
Cdd:PHA02878   149 ITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTD 228


                   ...
gi 1034644475 1307 QKD 1309
Cdd:PHA02878   229 ARD 231
PHA03095 PHA03095
ankyrin-like protein; Provisional
 498-594 1.34e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 59.65  E-value: 1.34e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475  498 ALHDDADLVHHCIKKGGNVNQPSYAGWTALHeasvggFYRTASE-------LLKGGADVNIKGLYQITPLHD--AVMNGH 568
Cdd:PHA03095    58 SSEKVKDIVRLLLEAGADVNAPERCGFTPLH------LYLYNATtldviklLIKAGADVNAKDKVGRTPLHVylSGFNIN 131

                           90       100
                   ....*....|....*....|....*.
gi 1034644475  569 YKVAELLLLNGADPLFRNDDGKCALD 594
Cdd:PHA03095   132 PKVIRLLLRKGADVNALDLYGMTPLA 157
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 1212-1306 1.64e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 58.85  E-value: 1.64e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475 1212 RGESQLHLAVRRGNLPLVKALIESGADVNLNDNAGWTPLHEASNEGSIDIIVELLKAGAKVNCENIDGILPLHDAVANNH 1291
Cdd:PHA02875   101 DGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGD 180

                           90
                   ....*....|....*
gi 1034644475 1292 LKAAEILLQNGANPN 1306
Cdd:PHA02875   181 IAICKMLLDSGANID 195
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 1199-1354 4.43e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 57.69  E-value: 4.43e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475 1199 LGMKAGRINKRNARG-ESQLHLAVRRGNLPLVKALIESGA---DVNLNDnaGWTPLHEASNEGSIDIIVELLKAGAKVNC 1274
Cdd:PHA02875    53 LLMKHGAIPDVKYPDiESELHDAVEEGDVKAVEELLDLGKfadDVFYKD--GMTPLHLATILKKLDIMKLLIARGADPDI 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475 1275 ENIDGILPLHDAVANNHLKAAEILLQNGANPNQKDQKQKS----ALDEADDEKMKELLRSYGAIETVNRDES-----DAI 1345
Cdd:PHA02875   131 PNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTpliiAMAKGDIAICKMLLDSGANIDYFGKNGCvaalcYAI 210


                   ....*....
gi 1034644475 1346 VNEKIPAVR 1354
Cdd:PHA02875   211 ENNKIDIVR 219
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1229-1309 6.90e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 57.34  E-value: 6.90e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475 1229 VKALIESGADVNLNDNAGWTPLH---EASNEGSIDIIVELLKAGAKVNCENIDGILPLHDAVAN-NHLKAAEILLQNGAN 1304
Cdd:PHA03095    30 VRRLLAAGADVNFRGEYGKTPLHlylHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNaTTLDVIKLLIKAGAD 109


                   ....*
gi 1034644475 1305 PNQKD 1309
Cdd:PHA03095   110 VNAKD 114
Ank_2 pfam12796
Ankyrin repeats (3 copies);
527-614 1.04e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 51.27  E-value: 1.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475  527 LHEASVGGFYRTASELLKGGADVNIKGLYQITPLHDAVMNGHYKVAELLLLNGAdpLFRNDDGKCALDEAKDL----CMK 602
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSghleIVK 78

                           90
                   ....*....|..
gi 1034644475  603 RLLERYIPKHQK 614
Cdd:pfam12796   79 LLLEKGADINVK 90
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1184-1306 1.40e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 56.19  E-value: 1.40e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475 1184 QNFRKRQSFLKTTCNLGMKAgriNKRNARGESQLHLAVRRGNL--PLVKALIESGADVNLNDNAGWTPLHEAS---NEGS 1258
Cdd:PHA03095   196 QSFKPRARIVRELIRAGCDP---AATDMLGNTPLHSMATGSSCkrSLVLPLLIAGISINARNRYGQTPLHYAAvfnNPRA 272

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1034644475 1259 IDiivELLKAGAKVNCENIDGILPLHDAVANNHLKAAEILLQngANPN 1306
Cdd:PHA03095   273 CR---RLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALA--KNPS 315
Ank_4 pfam13637
Ankyrin repeats (many copies);
1246-1299 3.76e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.42  E-value: 3.76e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1034644475 1246 GWTPLHEASNEGSIDIIVELLKAGAKVNCENIDGILPLHDAVANNHLKAAEILL 1299
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
1205-1253 4.54e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.50  E-value: 4.54e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1034644475 1205 RINKRNARGESQLHLAVRRGNLPLVKALIESGADVNLNDNAGWTPLHEA 1253
Cdd:pfam13857    8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1209-1306 5.80e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 54.26  E-value: 5.80e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475 1209 RNARGESQLH--LAVRRGNLPLVKALIESGADVNLNDNAGWTPLHEASNEGSID--IIVELLKAGAKVNCENIDGILPLH 1284
Cdd:PHA03095   183 VDDRFRSLLHhhLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPLH 262

                           90       100
                   ....*....|....*....|..
gi 1034644475 1285 DAVANNHLKAAEILLQNGANPN 1306
Cdd:PHA03095   263 YAAVFNNPRACRRLIALGADIN 284
Ank_4 pfam13637
Ankyrin repeats (many copies);
523-576 1.21e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.27  E-value: 1.21e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1034644475  523 GWTALHEASVGGFYRTASELLKGGADVNIKGLYQITPLHDAVMNGHYKVAELLL 576
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 1221-1322 1.35e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 53.53  E-value: 1.35e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475 1221 VRRGNLPLVKALIESGADVNLNDNAGWTPLHEASNEGSIDIIVELLKAGAKVNCENIDGILPLHDAVANNHLKAAEILLQ 1300
Cdd:PHA02876   153 IQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIID 232

                           90       100
                   ....*....|....*....|..
gi 1034644475 1301 NGANPNQKDQKQKSALDEADDE 1322
Cdd:PHA02876   233 NRSNINKNDLSLLKAIRNEDLE 254
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 542-596 2.41e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.59  E-value: 2.41e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1034644475  542 LLKGGADVNIKGLYQITPLHDAVMNGHYKVAELLLLNGADPLFRNDDGKCALDEA 596
Cdd:PTZ00322   101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA 155
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 1241-1329 3.69e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.82  E-value: 3.69e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475 1241 LNDNAGWTPLHEASNEGSID------IIVEL---------------LKAGAKVNCENIDGILPLHDAVANNHLKAAEILL 1299
Cdd:PTZ00322    56 ATENKDATPDHNLTTEEVIDpvvahmLTVELcqlaasgdavgarilLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLL 135

                           90       100       110
                   ....*....|....*....|....*....|
gi 1034644475 1300 QNGANPNQKDQKQKSALDEADDEKMKELLR 1329
Cdd:PTZ00322   136 EFGADPTLLDKDGKTPLELAEENGFREVVQ 165
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 1206-1339 1.17e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 48.28  E-value: 1.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475 1206 INKRNARGESQLH--LAVRRGNLPLVKALIESGADVN-LNDNAGWTPLHE--ASNEG-SIDIIVELLKAGAKVNCENIDG 1279
Cdd:PHA02859    44 VNDCNDLYETPIFscLEKDKVNVEILKFLIENGADVNfKTRDNNLSALHHylSFNKNvEPEILKILIDSGSSITEEDEDG 123

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034644475 1280 ILPLHDAVANNHLK--AAEILLQNGANPNQKDQKQKSALDE----ADDEKMKELLRSYGA-IETVNR 1339
Cdd:PHA02859   124 KNLLHMYMCNFNVRinVIKLLIDSGVSFLNKDFDNNNILYSyilfHSDKKIFDFLTSLGIdINETNK 190
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 1210-1329 1.19e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 50.25  E-value: 1.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475 1210 NARGESQLHLAVRRGNLPLVKALIESGADVNLNDNAGWTPL-------H------------------------EASNEGS 1258
Cdd:PLN03192   555 DSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnaisakHhkifrilyhfasisdphaagdllcTAAKRND 634

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034644475 1259 IDIIVELLKAGAKVNCENIDGILPLHDAVANNHLKAAEILLQNGAnpnqkDQKQKSALDEADDEKMKELLR 1329
Cdd:PLN03192   635 LTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGA-----DVDKANTDDDFSPTELRELLQ 700
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 1213-1333 1.49e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 49.60  E-value: 1.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475 1213 GESQLHLAVRRGNLPLVKALIESGADVNLNDNAGWTPLHEASNEGSIDIIVELLKAGAKVN-CENIDGILPLHDAVANNH 1291
Cdd:PHA02875    35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKK 114

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1034644475 1292 LKAAEILLQNGANPNQKDQKQKSALDEA---DDEKMKELLRSYGA 1333
Cdd:PHA02875   115 LDIMKLLIARGADPDIPNTDKFSPLHLAvmmGDIKGIELLIDHKA 159
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 1212-1333 1.56e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 49.49  E-value: 1.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475 1212 RGESQLHLAVRRGNLPLVKALIESGADVNLNDNAGWTPLHEASNEGSIDIIVELLKAGAKVNCENIDGILPLHDAVAN-N 1290
Cdd:PHA02878   167 KGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcK 246

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1034644475 1291 HLKAAEILLQNGANPNQKDQ-KQKSALDEA-DDEKMKELLRSYGA 1333
Cdd:PHA02878   247 DYDILKLLLEHGVDVNAKSYiLGLTALHSSiKSERKLKLLLEYGA 291
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 483-596 2.38e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 48.81  E-value: 2.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475  483 INRRNIFGENLVYKAALHDDADLVHHCIKKGGNVNQPSYAGWTALHEASVGGFYRTASELLKGGADVNIKGLYQITPLHD 562
Cdd:PHA02874   117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1034644475  563 AVMNGHYKVAELLLLNGADPLFRNDDGKCALDEA 596
Cdd:PHA02874   197 AAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA 230
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 1217-1340 2.59e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 49.11  E-value: 2.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475 1217 LHLAVRRGNLPLVKALIESGADVNLNDNAGWTPLHEASNEGSIDIIVELLKagAKVNCENIDGILPLHDAVANNHLKAAE 1296
Cdd:PHA02878    41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIR--SINKCSVFYTLVAIKDAFNNRNVEIFK 118

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1034644475 1297 ILLQNGANPNQK-DQKQ--KSALDEADDEKMKELLRSYGA-IETVNRD 1340
Cdd:PHA02878   119 IILTNRYKNIQTiDLVYidKKSKDDIIEAEITKLLLSYGAdINMKDRH 166
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 1206-1319 3.63e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.91  E-value: 3.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475 1206 INKRNARGESQLHLAVRRGNLP-LVKALIESGADVNLNDNAGWTPLH-EASNEGSIDIIVELLKAGAKVNCENIDGILPL 1283
Cdd:PHA02876   266 VNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYlMAKNGYDTENIRTLIMLGADVNAADRLYITPL 345

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1034644475 1284 HDAVANNHLKAAEI-LLQNGANPNQKDQKQKSALDEA 1319
Cdd:PHA02876   346 HQASTLDRNKDIVItLLELGANVNARDYCDKTPIHYA 382
Ank_5 pfam13857
Ankyrin repeats (many copies);
545-596 4.40e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.72  E-value: 4.40e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1034644475  545 GGADVNIKGLYQITPLHDAVMNGHYKVAELLLLNGADPLFRNDDGKCALDEA 596
Cdd:pfam13857    5 GPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 1229-1299 4.58e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.36  E-value: 4.58e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034644475 1229 VKALIESGADVNLNDNAGWTPLHEASNEGSIDIIVELLKAGAKVNCENIDGILPLHDAVANNHLKAAEILL 1299
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 537-598 9.32e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 47.37  E-value: 9.32e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034644475  537 RTASELLKGGADVNIKGLYQITPLHDAVMNGHYKVAELLLLNGADPLFRNDDGKCALDEAKD 598
Cdd:PHA02876   159 LIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVD 220
PHA03095 PHA03095
ankyrin-like protein; Provisional
 487-593 1.12e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.94  E-value: 1.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475  487 NIFGENLVYK---AALHDDADLVHHCIKKGGNVNQPSYAGWTALHEasvggFYRTASE--------LLKGGADVNIKGLY 555
Cdd:PHA03095     8 DIIMEAALYDyllNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHL-----YLHYSSEkvkdivrlLLEAGADVNAPERC 82

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1034644475  556 QITPLHDAVMNGH-YKVAELLLLNGADPLFRNDDGKCAL 593
Cdd:PHA03095    83 GFTPLHLYLYNATtLDVIKLLIKAGADVNAKDKVGRTPL 121
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 1209-1309 1.43e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 46.93  E-value: 1.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475 1209 RNARGESQLHLAVRRGNLPLVKALIESGAD-VNLNDN----AGWTPLHEASNEGSIDIIVELLKAGAKVNC--------- 1274
Cdd:cd22192     47 RGALGETALHVAALYDNLEAAVVLMEAAPElVNEPMTsdlyQGETALHIAVVNQNLNLVRELIARGADVVSpratgtffr 126

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1034644475 1275 ENIDGIL-----PLHDAVANNHLKAAEILLQNGANPNQKD 1309
Cdd:cd22192    127 PGPKNLIyygehPLSFAACVGNEEIVRLLIEHGADIRAQD 166
Ank_5 pfam13857
Ankyrin repeats (many copies);
1265-1319 1.56e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.18  E-value: 1.56e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034644475 1265 LLKAG-AKVNCENIDGILPLHDAVANNHLKAAEILLQNGANPNQKDQKQKSALDEA 1319
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 1140-1319 1.62e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.60  E-value: 1.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475 1140 HKPDEE----LTNNISGDEITIRNCEEikekteseihmptnSQEHKTVQNFRKRQSFLKTTCNLGMKAGRINKRNARGES 1215
Cdd:PHA02876   115 HKLDEAcihiLKEAISGNDIHYDKINE--------------SIEYMKLIKERIQQDELLIAEMLLEGGADVNAKDIYCIT 180

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475 1216 QLHLAVRRGNLPLVKALIESGADVNLNDNAGWTPLHEASNEGSIDIIVELLKAGAKVNCENidgiLPLHDAVANNHLKAA 1295
Cdd:PHA02876   181 PIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKND----LSLLKAIRNEDLETS 256

                          170       180
                   ....*....|....*....|....
gi 1034644475 1296 EILLQNGANPNQKDQKQKSALDEA 1319
Cdd:PHA02876   257 LLLYDAGFSVNSIDDCKNTPLHHA 280
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 1206-1321 2.27e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.21  E-value: 2.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475 1206 INKRNARGESQLHL--AVRRGNLPLVKALIESGADVNLNDNAGWTPLHEASNEGSIDIIV-ELLKAGAKVNCENIDGILP 1282
Cdd:PHA02876   231 IDNRSNINKNDLSLlkAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLVpKLLERGADVNAKNIKGETP 310

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1034644475 1283 LHDAVANNH-LKAAEILLQNGANPNQKDQ------KQKSALDEADD 1321
Cdd:PHA02876   311 LYLMAKNGYdTENIRTLIMLGADVNAADRlyitplHQASTLDRNKD 356
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 1246-1274 2.34e-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: 39.88  E-value: 2.34e-04
                            10        20
                    ....*....|....*....|....*....
gi 1034644475  1246 GWTPLHEASNEGSIDIIVELLKAGAKVNC 1274
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1278-1309 2.60e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.97  E-value: 2.60e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1034644475 1278 DGILPLHDAVA-NNHLKAAEILLQNGANPNQKD 1309
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
PHA03095 PHA03095
ankyrin-like protein; Provisional
 483-596 2.68e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 45.79  E-value: 2.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475  483 INRRNIFGENLVYkaaLHDDADLVHHCIKKGGNVNQPSYAGWTALHEASVGGFYRTA--SELLKGGADVNIKGLYQITPL 560
Cdd:PHA03095   185 DRFRSLLHHHLQS---FKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSlvLPLLIAGISINARNRYGQTPL 261

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1034644475  561 HDAVMNGHYKVAELLLLNGADPLFRNDDGKCALDEA 596
Cdd:PHA03095   262 HYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLM 297
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 558-587 2.81e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.97  E-value: 2.81e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1034644475  558 TPLHDAV-MNGHYKVAELLLLNGADPLFRND 587
Cdd:pfam00023    4 TPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA02917 PHA02917
ankyrin-like protein; Provisional
 1206-1291 3.14e-04

ankyrin-like protein; Provisional


Pssm-ID: 165231 [Multi-domain]  Cd Length: 661  Bit Score: 45.76  E-value: 3.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475 1206 INKRNARGESQLHLAVRRGNLPLVKALIESGADVNLNDNAGWTPLHEASNEG-SIDIIVELLKAGAKVNCEnIDGILPLH 1284
Cdd:PHA02917   445 INMIDKRGETLLHKAVRYNKQSLVSLLLESGSDVNIRSNNGYTCIAIAINESrNIELLKMLLCHKPTLDCV-IDSLREIS 523


                   ....*..
gi 1034644475 1285 DAVANNH 1291
Cdd:PHA02917   524 NIVDNAY 530
PHA02798 PHA02798
ankyrin-like protein; Provisional
 1185-1276 3.46e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 45.21  E-value: 3.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475 1185 NFRKRQSFLKTTCNLGMKAGRINKRNARGESQLHLAVRRG---NLPLVKALIESGADVNLNDNAGWTPLH---EASNEGS 1258
Cdd:PHA02798    81 NIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGyinNLEILLFMIENGADTTLLDKDGFTMLQvylQSNHHID 160

                           90
                   ....*....|....*...
gi 1034644475 1259 IDIIVELLKAGAKVNCEN 1276
Cdd:PHA02798   161 IEIIKLLLEKGVDINTHN 178
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 483-581 4.05e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.44  E-value: 4.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475  483 INRRNIFGENLVYKAALHD-DADLVHHCIKKGGNVNQPSYAGWTALHEASVGGFYR-TASELLKGGADVNIKGLYQITPL 560
Cdd:PHA02876   300 VNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKdIVITLLELGANVNARDYCDKTPI 379

                           90       100
                   ....*....|....*....|.
gi 1034644475  561 HDAVMNGHYKVAELLLLNGAD 581
Cdd:PHA02876   380 HYAAVRNNVVIINTLLDYGAD 400
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 1212-1241 4.31e-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: 39.11  E-value: 4.31e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 1034644475  1212 RGESQLHLAVRRGNLPLVKALIESGADVNL 1241
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
RAMA pfam18755
Restriction Enzyme Adenine Methylase Associated; An alpha+beta fold domain associated with ...
 1739-1778 4.36e-04

Restriction Enzyme Adenine Methylase Associated; An alpha+beta fold domain associated with restriction enzymes across prokaryotes and fused to JAB deubiquitinases, and chromatin proteins in a wide range of eukaryotes. The domain is predicted to function as a modified-DNA reader domain.


Pssm-ID: 465856  Cd Length: 108  Bit Score: 41.53  E-value: 4.36e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1034644475 1739 TIKKALNYSTAPKKKCIQIKDLILLGRINPGNNIL--EFKTQ 1778
Cdd:pfam18755    3 SESAPSGGSSRRTGRRVTLQDLLEAGLLQPGEGLLsiEYKGQ 44
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1246-1276 4.59e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.19  E-value: 4.59e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1034644475 1246 GWTPLHEAS-NEGSIDIIVELLKAGAKVNCEN 1276
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 1278-1306 4.89e-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: 39.11  E-value: 4.89e-04
                            10        20
                    ....*....|....*....|....*....
gi 1034644475  1278 DGILPLHDAVANNHLKAAEILLQNGANPN 1306
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1217-1244 5.43e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.19  E-value: 5.43e-04
                           10        20
                   ....*....|....*....|....*....
gi 1034644475 1217 LHLAV-RRGNLPLVKALIESGADVNLNDN 1244
Cdd:pfam00023    6 LHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 475-596 5.65e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 44.66  E-value: 5.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475  475 VNKISLHSINRRNIFGENLVYKAAL-------HDDADLVHHCIKKGGNVNQPSYAGWTALHEASVGGFY-----RTASEL 542
Cdd:PHA03100    13 IKVKNIKYIIMEDDLNDYSYKKPVLplylakeARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLL 92

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034644475  543 LKGGADVNIKGLYQITPLHDAVMN--GHYKVAELLLLNGADPLFRNDDGKCALDEA 596
Cdd:PHA03100    93 LEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLY 148
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 555-582 6.07e-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: 38.72  E-value: 6.07e-04
                            10        20
                    ....*....|....*....|....*...
gi 1034644475   555 YQITPLHDAVMNGHYKVAELLLLNGADP 582
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 1207-1266 6.43e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.50  E-value: 6.43e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475 1207 NKRNARGESQLHLAVRRGNLPLVKALIESGADVNLNDNAGWTPLHEASNEGSIDiIVELL 1266
Cdd:PTZ00322   109 NCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFRE-VVQLL 167
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 482-581 8.63e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 44.28  E-value: 8.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475  482 SINRRNIFGENLVYKAALHDDADLVHHCIKKGGNVNQPSYAGWTALHEASVG-GFYRTASELLKGGADVNIKGLYQITPL 560
Cdd:PHA02876   367 NVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGtNPYMSVKTLIDRGANVNSKNKDLSTPL 446

                           90       100
                   ....*....|....*....|..
gi 1034644475  561 HDAVMNG-HYKVAELLLLNGAD 581
Cdd:PHA02876   447 HYACKKNcKLDVIEMLLDNGAD 468
Ank_5 pfam13857
Ankyrin repeats (many copies);
1232-1284 8.91e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.25  E-value: 8.91e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1034644475 1232 LIESG-ADVNLNDNAGWTPLHEASNEGSIDIIVELLKAGAKVNCENIDGILPLH 1284
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
558-596 1.03e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.79  E-value: 1.03e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1034644475  558 TPLHDAVMNGHYKVAELLLLNGADPLFRNDDGKCALDEA 596
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFA 41
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1217-1240 1.71e-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: 37.62  E-value: 1.71e-03
                           10        20
                   ....*....|....*....|....
gi 1034644475 1217 LHLAVRRGNLPLVKALIESGADVN 1240
Cdd:pfam13606    6 LHLAARNGRLEIVKLLLENGADIN 29
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 1212-1333 1.71e-03

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 43.33  E-value: 1.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475 1212 RGESQLHLAVRRGNLPLVKALIESGADVNLNDNA-------------GWTPLHEASNEGSIDIIVELLKAGAKVNCenid 1278
Cdd:cd21882     72 QGQTALHIAIENRNLNLVRLLVENGADVSARATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPAA---- 147

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1034644475 1279 giLPLHDAVANNHLKAaeILLQnganPNQKDQKQKSALdeaddeKMKELLRSYGA 1333
Cdd:cd21882    148 --LEAQDSLGNTVLHA--LVLQ----ADNTPENSAFVC------QMYNLLLSYGA 188
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1283-1316 2.59e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 38.94  E-value: 2.59e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1034644475 1283 LHDAVANNHLKAAEILLQNGANPNQKDQKQKSAL 1316
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTAL 34
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 486-588 3.22e-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: 42.31  E-value: 3.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475  486 RNIFGENLVYKAALHDDADLVHHCIKKG-GNVNQPS----YAGWTALHEASVGGFYRTASELLKGGADV----------- 549
Cdd:cd22192     47 RGALGETALHVAALYDNLEAAVVLMEAApELVNEPMtsdlYQGETALHIAVVNQNLNLVRELIARGADVvspratgtffr 126

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1034644475  550 -NIKGL--YQITPLHDAVMNGHYKVAELLLLNGADPlfRNDD 588
Cdd:cd22192    127 pGPKNLiyYGEHPLSFAACVGNEEIVRLLIEHGADI--RAQD 166
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 483-596 3.41e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 41.87  E-value: 3.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475  483 INRRNIFGENLVYKAALHDDADLVHHCIKKGGNVNQPSYAGWTALHEASVGGFYRTASELLKGGADVNIKGLYQITPLHD 562
Cdd:PHA02874   150 VNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHN 229

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1034644475  563 AVMngHYKVAELLLLNGADPLFRNDDGKCALDEA 596
Cdd:PHA02874   230 AII--HNRSAIELLINNASINDQDIDGSTPLHHA 261
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 1213-1284 3.45e-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: 42.31  E-value: 3.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475 1213 GESQLHLAVRRGNLPLVKALIESGADVnLNDNA---------------GWTPLHEASNEGSIDIIVELLKAGAKVNCENI 1277
Cdd:cd22192     89 GETALHIAVVNQNLNLVRELIARGADV-VSPRAtgtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDS 167


                   ....*..
gi 1034644475 1278 DGILPLH 1284
Cdd:cd22192    168 LGNTVLH 174
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 483-582 4.39e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 41.79  E-value: 4.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475  483 INRRNIFGENLVYKAALHDDADLVHHCIKKGGNVNQPSYAGWTALHeASVGGF--YRTASELLKGGADVNIKG-LYQITP 559
Cdd:PHA02878   194 VNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLH-ISVGYCkdYDILKLLLEHGVDVNAKSyILGLTA 272

                           90       100
                   ....*....|....*....|...
gi 1034644475  560 LHDAVMNGhyKVAELLLLNGADP 582
Cdd:PHA02878   273 LHSSIKSE--RKLKLLLEYGADI 293
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1222-1333 4.86e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 41.57  E-value: 4.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475 1222 RRGNLPLVKALIESGADVNLNDNAGWTPLHEASNEGSIDIIVELLKAGAKVNCENIDGILPLH-----DAVANNHLKAAE 1296
Cdd:PHA03100    11 RIIKVKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVK 90

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1034644475 1297 ILLQNGANPNQKDQKQKSALDEADDEKMK-----ELLRSYGA 1333
Cdd:PHA03100    91 LLLEYGANVNAPDNNGITPLLYAISKKSNsysivEYLLDNGA 132
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 493-581 4.90e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 41.57  E-value: 4.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475  493 LVYKAALHDDADLVHHCIKKGGNVNQPSYAGWTALHEASVG--GFYRTASELLKGGADVNIKGLYQITPLHDAVMNGHY- 569
Cdd:PHA03100    76 SNIKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKId 155

                           90
                   ....*....|...
gi 1034644475  570 -KVAELLLLNGAD 581
Cdd:PHA03100   156 lKILKLLIDKGVD 168
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 1229-1303 5.45e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 41.59  E-value: 5.45e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034644475 1229 VKALIESGADVNLNDNAGWTPLHEA-SNEGSIDIIVELLKAGAKVNCENIDGILPLhdAVANNHLKAAEILLQNGA 1303
Cdd:PHA02876   425 VKTLIDRGANVNSKNKDLSTPLHYAcKKNCKLDVIEMLLDNGADVNAINIQNQYPL--LIALEYHGIVNILLHYGA 498
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 1212-1306 5.64e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 41.27  E-value: 5.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475 1212 RGESQLHLAVRRGNLP--LVKALIESGADVNLNdnaGW--TPLHEASNEGSID------IIVELLKAGAKVNCENIDGIL 1281
Cdd:PHA02989    34 RGNSILLLYLKRKDVKikIVKLLIDNGADVNYK---GYieTPLCAVLRNREITsnkikkIVKLLLKFGADINLKTFNGVS 110

                           90       100
                   ....*....|....*....|....*...
gi 1034644475 1282 PLHDAVANNHLKAAEIL---LQNGANPN 1306
Cdd:PHA02989   111 PIVCFIYNSNINNCDMLrflLSKGINVN 138
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 502-607 5.73e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 41.40  E-value: 5.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644475  502 DADLVHHCIKKGGNVNQPS-YAGWTALHEASVGGFYRTASELLKGGADVNIKGLYQITPLHDAVMNGHYKVAELLLLNGA 580
Cdd:PHA02878   146 EAEITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1034644475  581 DPLFRNDDGKCALDEAKDLC-----MKRLLER 607
Cdd:PHA02878   226 STDARDKCGNTPLHISVGYCkdydiLKLLLEH 257
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1246-1274 6.25e-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: 36.08  E-value: 6.25e-03
                           10        20
                   ....*....|....*....|....*....
gi 1034644475 1246 GWTPLHEASNEGSIDIIVELLKAGAKVNC 1274
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
492-543 8.66e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.10  E-value: 8.66e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1034644475  492 NLVYKAALHDDADLVHHCIKKGGNVNQPSYAGWTALHEASVGGFYRTASELL 543
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
1282-1319 9.10e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.10  E-value: 9.10e-03
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1034644475 1282 PLHDAVANNHLKAAEILLQNGANPNQKDQKQKSALDEA 1319
Cdd:pfam13637    4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFA 41
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 523-552 9.70e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.34  E-value: 9.70e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1034644475  523 GWTALHEASV-GGFYRTASELLKGGADVNIK 552
Cdd:pfam00023    2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNAR 32
 
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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