NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|41054155|ref|NP_956131|]
View 

protein fem-1 homolog A [Danio rerio]

Protein Classification

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

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

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
2-251 1.39e-43

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 157.81  E-value: 1.39e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155   2 DISAAVFNAARDGKLKLMQKLLINKSpeerAALAEERTEGGTPLLIAARYGHLPVVHFLLERcGANVALggsVNFDGETi 81
Cdd:COG0666  52 ALGALLLLAAALAGDLLVALLLLAAG----ADINAKDDGGNTLLHAAARNGDLEIVKLLLEA-GADVNA---RDKDGET- 122

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155  82 egapPLWAASAAGHLPVVKALLEHGAPVNNTTLTNSTPLRAACFDGHLEIVRYLVEHQADLEVANRHGHTCLMISCYKGH 161
Cdd:COG0666 123 ----PLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGH 198

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155 162 REIAQFLLEKGADVNRKSVKGNTALHDCAESGSLEIMKMLLKCDARME-RDGYGMTPLLAASVTGHTNIVEFLVHQPRAS 240
Cdd:COG0666 199 LEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNaKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278

                       250
                ....*....|.
gi 41054155 241 REQRIHALELL 251
Cdd:COG0666 279 AAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
476-579 1.77e-15

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 77.30  E-value: 1.77e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155 476 LNPRARGGHTPLHMAVDRDttsvgrypvgrfpSLAVASLLLECGADVDSRDYDNNTPLHIAAANGCPDIMAALIRAGAHF 555
Cdd:COG0666 113 VNARDKDGETPLHLAAYNG-------------NLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADV 179

                        90       100
                ....*....|....*....|....
gi 41054155 556 DATNAAQQTAyqLLEAQSSGRHAL 579
Cdd:COG0666 180 NARDNDGETP--LHLAAENGHLEI 201
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
2-251 1.39e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 157.81  E-value: 1.39e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155   2 DISAAVFNAARDGKLKLMQKLLINKSpeerAALAEERTEGGTPLLIAARYGHLPVVHFLLERcGANVALggsVNFDGETi 81
Cdd:COG0666  52 ALGALLLLAAALAGDLLVALLLLAAG----ADINAKDDGGNTLLHAAARNGDLEIVKLLLEA-GADVNA---RDKDGET- 122

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155  82 egapPLWAASAAGHLPVVKALLEHGAPVNNTTLTNSTPLRAACFDGHLEIVRYLVEHQADLEVANRHGHTCLMISCYKGH 161
Cdd:COG0666 123 ----PLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGH 198

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155 162 REIAQFLLEKGADVNRKSVKGNTALHDCAESGSLEIMKMLLKCDARME-RDGYGMTPLLAASVTGHTNIVEFLVHQPRAS 240
Cdd:COG0666 199 LEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNaKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278

                       250
                ....*....|.
gi 41054155 241 REQRIHALELL 251
Cdd:COG0666 279 AAALLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
87-178 1.97e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 91.72  E-value: 1.97e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155    87 LWAASAAGHLPVVKALLEHGAPVNNTTLTNSTPLRAACFDGHLEIVRYLVEHqADLEVANrHGHTCLMISCYKGHREIAQ 166
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 41054155   167 FLLEKGADVNRK 178
Cdd:pfam12796  79 LLLEKGADINVK 90
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 98-236 7.97e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 80.09  E-value: 7.97e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155   98 VVKALLEHGAPVNNTTLTNSTPLRAACFDGH-----LEIVRYLVEHQADLEVANRHGHTCLM--ISCYKGHREIAQFLLE 170
Cdd:PHA03100  50 VVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITPLLyaISKKSNSYSIVEYLLD 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155  171 KGADVNRKSVKGNTALHDCAESGS--LEIMKMLLKCDARM-----------------ERDGYGMTPLLAASVTGHTNIVE 231
Cdd:PHA03100 130 NGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDInaknrvnyllsygvpinIKDVYGFTPLHYAVYNNNPEFVK 209


                 ....*
gi 41054155  232 FLVHQ 236
Cdd:PHA03100 210 YLLDL 214
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
476-579 1.77e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 77.30  E-value: 1.77e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155 476 LNPRARGGHTPLHMAVDRDttsvgrypvgrfpSLAVASLLLECGADVDSRDYDNNTPLHIAAANGCPDIMAALIRAGAHF 555
Cdd:COG0666 113 VNARDKDGETPLHLAAYNG-------------NLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADV 179

                        90       100
                ....*....|....*....|....
gi 41054155 556 DATNAAQQTAyqLLEAQSSGRHAL 579
Cdd:COG0666 180 NARDNDGETP--LHLAAENGHLEI 201
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 7-239 4.45e-11

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: 65.80  E-value: 4.45e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155   7 VFNAARDGKLKLMQKLLINKS--PEERAALAEerteggTPLLIAARYGHLPVVHFLLE--RCGANVALGGSVnFDGETie 82
Cdd:cd22192  21 LLLAAKENDVQAIKKLLKCPScdLFQRGALGE------TALHVAALYDNLEAAVVLMEaaPELVNEPMTSDL-YQGET-- 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155  83 gapPLWAASAAGHLPVVKALLEHGAPVNNTTLTNStplraaCFDGHLEIVRYLVEHQadLEVAnrhghTCLmiscykGHR 162
Cdd:cd22192  92 ---ALHIAVVNQNLNLVRELIARGADVVSPRATGT------FFRPGPKNLIYYGEHP--LSFA-----ACV------GNE 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155 163 EIAQFLLEKGADVNRKSVKGNTALHDCA----ESGSLEIMKMLLKCDAR-------MERDGYGMTPLLAASVTGHTNIVE 231
Cdd:cd22192 150 EIVRLLIEHGADIRAQDSLGNTVLHILVlqpnKTFACQMYDLILSYDKEddlqpldLVPNNQGLTPFKLAAKEGNIVMFQ 229


                ....*...
gi 41054155 232 FLVHQPRA 239
Cdd:cd22192 230 HLVQKRRH 237
Ank_2 pfam12796
Ankyrin repeats (3 copies);
469-559 3.21e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 48.57  E-value: 3.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155   469 TVYRLLKLNPRARG----GHTPLHMAVDRDttsvgrypvgrfpSLAVASLLLECgADVDSRDYdNNTPLHIAAANGCPDI 544
Cdd:pfam12796  12 LVKLLLENGADANLqdknGRTALHLAAKNG-------------HLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEI 76

                          90
                  ....*....|....*
gi 41054155   545 MAALIRAGAHFDATN 559
Cdd:pfam12796  77 VKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 476-560 1.00e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 51.56  E-value: 1.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155  476 LNPRARGGHTPLHMAVDRDTTsvgrypvgrfpsLAVASLLLECGADVDSRDYDNNTPLHIAAANGC--PDIMAALIRAGA 553
Cdd:PHA03095  76 VNAPERCGFTPLHLYLYNATT------------LDVIKLLIKAGADVNAKDKVGRTPLHVYLSGFNinPKVIRLLLRKGA 143


                 ....*..
gi 41054155  554 HFDATNA 560
Cdd:PHA03095 144 DVNALDL 150
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 148-176 3.94e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 40.65  E-value: 3.94e-05
                           10        20
                   ....*....|....*....|....*....
gi 41054155    148 HGHTCLMISCYKGHREIAQFLLEKGADVN 176
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 468-553 1.64e-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: 41.54  E-value: 1.64e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155 468 QTVYRLLK---LNPRARG--GHTPLHMAVDRDttsvgrypvgrfpSLAVASLLLECGAD-----VDSRDYDNNTPLHIAA 537
Cdd:cd22192  31 QAIKKLLKcpsCDLFQRGalGETALHVAALYD-------------NLEAAVVLMEAAPElvnepMTSDLYQGETALHIAV 97

                        90
                ....*....|....*.
gi 41054155 538 ANGCPDIMAALIRAGA 553
Cdd:cd22192  98 VNQNLNLVRELIARGA 113
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 528-557 2.97e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.64  E-value: 2.97e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 41054155    528 DNNTPLHIAAANGCPDIMAALIRAGAHFDA 557
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
2-251 1.39e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 157.81  E-value: 1.39e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155   2 DISAAVFNAARDGKLKLMQKLLINKSpeerAALAEERTEGGTPLLIAARYGHLPVVHFLLERcGANVALggsVNFDGETi 81
Cdd:COG0666  52 ALGALLLLAAALAGDLLVALLLLAAG----ADINAKDDGGNTLLHAAARNGDLEIVKLLLEA-GADVNA---RDKDGET- 122

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155  82 egapPLWAASAAGHLPVVKALLEHGAPVNNTTLTNSTPLRAACFDGHLEIVRYLVEHQADLEVANRHGHTCLMISCYKGH 161
Cdd:COG0666 123 ----PLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGH 198

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155 162 REIAQFLLEKGADVNRKSVKGNTALHDCAESGSLEIMKMLLKCDARME-RDGYGMTPLLAASVTGHTNIVEFLVHQPRAS 240
Cdd:COG0666 199 LEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNaKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278

                       250
                ....*....|.
gi 41054155 241 REQRIHALELL 251
Cdd:COG0666 279 AAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-233 3.90e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 150.87  E-value: 3.90e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155   1 MDISAAVFNAARDGKLKLMQKLLINKSPEERAALAEERTEGGTPLLIAARYGHLPVVHFLLERCGANValggsvnfDGET 80
Cdd:COG0666  13 AALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI--------NAKD 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155  81 IEGAPPLWAASAAGHLPVVKALLEHGAPVNNTTLTNSTPLRAACFDGHLEIVRYLVEHQADLEVANRHGHTCLMISCYKG 160
Cdd:COG0666  85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANG 164

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41054155 161 HREIAQFLLEKGADVNRKSVKGNTALHDCAESGSLEIMKMLLKCDARME-RDGYGMTPLLAASVTGHTNIVEFL 233
Cdd:COG0666 165 NLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNaKDNDGKTALDLAAENGNLEIVKLL 238
Ank_2 pfam12796
Ankyrin repeats (3 copies);
87-178 1.97e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 91.72  E-value: 1.97e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155    87 LWAASAAGHLPVVKALLEHGAPVNNTTLTNSTPLRAACFDGHLEIVRYLVEHqADLEVANrHGHTCLMISCYKGHREIAQ 166
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 41054155   167 FLLEKGADVNRK 178
Cdd:pfam12796  79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
120-210 7.73e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 81.70  E-value: 7.73e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155   120 LRAACFDGHLEIVRYLVEHQADLEVANRHGHTCLMISCYKGHREIAQFLLEKgADVNRKSvKGNTALHDCAESGSLEIMK 199
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|.
gi 41054155   200 MLLKCDARMER 210
Cdd:pfam12796  79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
153-235 4.29e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.39  E-value: 4.29e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155   153 LMISCYKGHREIAQFLLEKGADVNRKSVKGNTALHDCAESGSLEIMKMLLKCdARMERDGYGMTPLLAASVTGHTNIVEF 232
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGRTALHYAARSGHLEIVKL 79


                  ...
gi 41054155   233 LVH 235
Cdd:pfam12796  80 LLE 82
Ank_2 pfam12796
Ankyrin repeats (3 copies);
45-146 3.02e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.00  E-value: 3.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155    45 LLIAARYGHLPVVHFLLErCGANValgGSVNFDGETiegapPLWAASAAGHLPVVKALLEHGAPvnNTTLTNSTPLRAAC 124
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLE-NGADA---NLQDKNGRT-----ALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAA 69

                          90       100
                  ....*....|....*....|..
gi 41054155   125 FDGHLEIVRYLVEHQADLEVAN 146
Cdd:pfam12796  70 RSGHLEIVKLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 98-236 7.97e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 80.09  E-value: 7.97e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155   98 VVKALLEHGAPVNNTTLTNSTPLRAACFDGH-----LEIVRYLVEHQADLEVANRHGHTCLM--ISCYKGHREIAQFLLE 170
Cdd:PHA03100  50 VVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITPLLyaISKKSNSYSIVEYLLD 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155  171 KGADVNRKSVKGNTALHDCAESGS--LEIMKMLLKCDARM-----------------ERDGYGMTPLLAASVTGHTNIVE 231
Cdd:PHA03100 130 NGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDInaknrvnyllsygvpinIKDVYGFTPLHYAVYNNNPEFVK 209


                 ....*
gi 41054155  232 FLVHQ 236
Cdd:PHA03100 210 YLLDL 214
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
476-579 1.77e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 77.30  E-value: 1.77e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155 476 LNPRARGGHTPLHMAVDRDttsvgrypvgrfpSLAVASLLLECGADVDSRDYDNNTPLHIAAANGCPDIMAALIRAGAHF 555
Cdd:COG0666 113 VNARDKDGETPLHLAAYNG-------------NLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADV 179

                        90       100
                ....*....|....*....|....
gi 41054155 556 DATNAAQQTAyqLLEAQSSGRHAL 579
Cdd:COG0666 180 NARDNDGETP--LHLAAENGHLEI 201
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 40-204 6.36e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 77.01  E-value: 6.36e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155   40 EGGTPLLIAA--RYGHLPVVHFLLERcGANVALggsVNFDGETIegaPPLWAASAAGHLPVVKALLEHGAPVNNTTltns 117
Cdd:PHA03100 105 NGITPLLYAIskKSNSYSIVEYLLDN-GANVNI---KNSDGENL---LHLYLESNKIDLKILKLLIDKGVDINAKN---- 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155  118 tplraacfdghleIVRYLVEHQADLEVANRHGHTCLMISCYKGHREIAQFLLEKGADVNRKSVKGNTALHDCAESGSLEI 197
Cdd:PHA03100 174 -------------RVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEI 240


                 ....*..
gi 41054155  198 MKMLLKC 204
Cdd:PHA03100 241 FKLLLNN 247
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
476-579 2.17e-14

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 74.22  E-value: 2.17e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155 476 LNPRARGGHTPLHMAVDRDttsvgrypvgrfpSLAVASLLLECGADVDSRDYDNNTPLHIAAANGCPDIMAALIRAGAHF 555
Cdd:COG0666 146 VNAQDNDGNTPLHLAAANG-------------NLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADV 212

                        90       100
                ....*....|....*....|....
gi 41054155 556 DATNAAQQTAyqLLEAQSSGRHAL 579
Cdd:COG0666 213 NAKDNDGKTA--LDLAAENGNLEI 234
PHA03095 PHA03095
ankyrin-like protein; Provisional
 68-218 1.09e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 73.52  E-value: 1.09e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155   68 VALGGSVNFDGETIEGAPPLWAASAAGHLP-VVKALLEHGAPVNNTTLTNSTPLRA-ACFDGHLEIVRYLVEHQADLEVA 145
Cdd:PHA03095  34 LAAGADVNFRGEYGKTPLHLYLHYSSEKVKdIVRLLLEAGADVNAPERCGFTPLHLyLYNATTLDVIKLLIKAGADVNAK 113

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41054155  146 NRHGHTCLMIsCYKG---HREIAQFLLEKGADVNRKSVKGNTALHDCAESG--SLEIMKMLLKCDARM-ERDGYGMTPL 218
Cdd:PHA03095 114 DKVGRTPLHV-YLSGfniNPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRnaNVELLRLLIDAGADVyAVDDRFRSLL 191
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 96-234 1.14e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 73.16  E-value: 1.14e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155   96 LPVVKALLEHGAPVNNTTLTNSTPLRAACFD--GHLEIVRYLVEHQADLEVANRHGHTCLMI--SCYKGHREIAQFLLEK 171
Cdd:PHA03100  86 KEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLylESNKIDLKILKLLIDK 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155  172 GADVNRKS----------------VKGNTALHDCAESGSLEIMKMLLKCDARME-RDGYGMTPLLAASVTGHTNIVEFLV 234
Cdd:PHA03100 166 GVDINAKNrvnyllsygvpinikdVYGFTPLHYAVYNNNPEFVKYLLDLGANPNlVNKYGDTPLHIAILNNNKEIFKLLL 245
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 14-235 1.26e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 66.91  E-value: 1.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155   14 GKLKLMQKLLINKSpeerAALAEERTEGGTPLLIAARYGHLPVVHFLLERcganvalGGSVNFDGETIEGaPPLWAASAA 93
Cdd:PHA02874  12 GDIEAIEKIIKNKG----NCINISVDETTTPLIDAIRSGDAKIVELFIKH-------GADINHINTKIPH-PLLTAIKIG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155   94 GH---------------LPV-------VKALLEHGAPVNNTTLTNSTPLRAACFDGHLEIVRYLVEHQADLEVANRHGHT 151
Cdd:PHA02874  80 AHdiikllidngvdtsiLPIpciekdmIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCY 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155  152 CLMISCYKGHREIAQFLLEKGADVNRKSVKGNTALHDCAESGSLEIMKMLLKCDAR-MERDGYGMTPLLAAsVTGHTNIV 230
Cdd:PHA02874 160 PIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHiMNKCKNGFTPLHNA-IIHNRSAI 238


                 ....*
gi 41054155  231 EFLVH 235
Cdd:PHA02874 239 ELLIN 243
Ank_2 pfam12796
Ankyrin repeats (3 copies);
10-110 1.26e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 60.90  E-value: 1.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155    10 AARDGKLKLMQKLLinkspEERAALAEERTEGGTPLLIAARYGHLPVVHFLLERCGANvalggsVNFDGETiegapPLWA 89
Cdd:pfam12796   4 AAKNGNLELVKLLL-----ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN------LKDNGRT-----ALHY 67

                          90       100
                  ....*....|....*....|.
gi 41054155    90 ASAAGHLPVVKALLEHGAPVN 110
Cdd:pfam12796  68 AARSGHLEIVKLLLEKGADIN 88
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
476-576 1.62e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 65.36  E-value: 1.62e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155 476 LNPRARGGHTPLHMAVDRDttsvgrypvgrfpSLAVASLLLECGADVDSRDYDNNTPLHIAAANGCPDIMAALIRAGAHF 555
Cdd:COG0666  80 INAKDDGGNTLLHAAARNG-------------DLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADV 146

                        90       100
                ....*....|....*....|.
gi 41054155 556 DATNAAQQTAyqLLEAQSSGR 576
Cdd:COG0666 147 NAQDNDGNTP--LHLAAANGN 165
PHA03095 PHA03095
ankyrin-like protein; Provisional
 98-218 1.88e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 66.59  E-value: 1.88e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155   98 VVKALLEHGAPVNNTTLTNSTPL----RAACFDGhLEIVRYLVEHQADLEVANRHGHT---CLMisCYKGHREIAQFLLE 170
Cdd:PHA03095  29 EVRRLLAAGADVNFRGEYGKTPLhlylHYSSEKV-KDIVRLLLEAGADVNAPERCGFTplhLYL--YNATTLDVIKLLIK 105

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 41054155  171 KGADVNRKSVKGNTALHDCAESGSL--EIMKMLLKCDARME-RDGYGMTPL 218
Cdd:PHA03095 106 AGADVNAKDKVGRTPLHVYLSGFNInpKVIRLLLRKGADVNaLDLYGMTPL 156
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
96-234 2.11e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 64.98  E-value: 2.11e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155  96 LPVVKALLEHGAPVNNTTLTNSTPLRAACFDGHLEIVRYLVEHQADLEVANRHGHTCLMISCYKGHREIAQFLLEKGADV 175
Cdd:COG0666   1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155 176 NRKSVKGNTALHDCAESGSLEIMKMLLKCDARME-RDGYGMTPLLAASVTGHTNIVEFLV 234
Cdd:COG0666  81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNaRDKDGETPLHLAAYNGNLEIVKLLL 140
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 7-239 4.45e-11

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: 65.80  E-value: 4.45e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155   7 VFNAARDGKLKLMQKLLINKS--PEERAALAEerteggTPLLIAARYGHLPVVHFLLE--RCGANVALGGSVnFDGETie 82
Cdd:cd22192  21 LLLAAKENDVQAIKKLLKCPScdLFQRGALGE------TALHVAALYDNLEAAVVLMEaaPELVNEPMTSDL-YQGET-- 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155  83 gapPLWAASAAGHLPVVKALLEHGAPVNNTTLTNStplraaCFDGHLEIVRYLVEHQadLEVAnrhghTCLmiscykGHR 162
Cdd:cd22192  92 ---ALHIAVVNQNLNLVRELIARGADVVSPRATGT------FFRPGPKNLIYYGEHP--LSFA-----ACV------GNE 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155 163 EIAQFLLEKGADVNRKSVKGNTALHDCA----ESGSLEIMKMLLKCDAR-------MERDGYGMTPLLAASVTGHTNIVE 231
Cdd:cd22192 150 EIVRLLIEHGADIRAQDSLGNTVLHILVlqpnKTFACQMYDLILSYDKEddlqpldLVPNNQGLTPFKLAAKEGNIVMFQ 229


                ....*...
gi 41054155 232 FLVHQPRA 239
Cdd:cd22192 230 HLVQKRRH 237
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 23-245 2.44e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 63.54  E-value: 2.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155   23 LINKSPEERAALAEERTEGGTPLLIAARYGhlpvvhFLLERCGANVALGGSVNfDGETIEGAPPLWAASAAGHLPVVKAL 102
Cdd:PHA02876 289 LVPKLLERGADVNAKNIKGETPLYLMAKNG------YDTENIRTLIMLGADVN-AADRLYITPLHQASTLDRNKDIVITL 361

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155  103 LEHGAPVNNTTLTNSTPLRAACFDGHLEIVRYLVEHQADLEVANRHGHTCLMISCYKGHREIA-QFLLEKGADVNRKSVK 181
Cdd:PHA02876 362 LELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMSvKTLIDRGANVNSKNKD 441

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41054155  182 GNTALH-DCAESGSLEIMKMLLKCDARME----RDGYgmtPLLAAsvTGHTNIVEFLVHQPRASREQRI 245
Cdd:PHA02876 442 LSTPLHyACKKNCKLDVIEMLLDNGADVNainiQNQY---PLLIA--LEYHGIVNILLHYGAELRDSRV 505
PHA03095 PHA03095
ankyrin-like protein; Provisional
 41-227 3.05e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 62.73  E-value: 3.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155   41 GGTPLLIAARYGH-LPVVHFLLeRCGANVALGGSVnfdGETiegapPL--WAASAAGHLPVVKALLEHGAPVNNTTLTNS 117
Cdd:PHA03095  83 GFTPLHLYLYNATtLDVIKLLI-KAGADVNAKDKV---GRT-----PLhvYLSGFNINPKVIRLLLRKGADVNALDLYGM 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155  118 TPLraACF----DGHLEIVRYLVEHQADLEVANRHGHTCLMISC--YKGHREIAQFLLEKGADVNRKSVKGNTALHDCAE 191
Cdd:PHA03095 154 TPL--AVLlksrNANVELLRLLIDAGADVYAVDDRFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLHSMAT 231

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 41054155  192 SGS---LEIMKMLLKCDARMERDGYGMTPLLAASVTGHT 227
Cdd:PHA03095 232 GSSckrSLVLPLLIAGISINARNRYGQTPLHYAAVFNNP 270
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 82-203 6.70e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.55  E-value: 6.70e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155   82 EGAPPLWAASAAGHLPVVKALLEHGAPVNNTTLTNSTPLRAACFDGHLEIVRYLVEHQADLEVANRHGHTCLMISCYKGH 161
Cdd:PHA02875 101 DGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGD 180

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 41054155  162 REIAQFLLEKGADVNRKSVKGN-TALHDCAESGSLEIMKMLLK 203
Cdd:PHA02875 181 IAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIK 223
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 3-203 9.54e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 61.81  E-value: 9.54e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155    3 ISAAVFNAARDGKLKLMQKLLinkspeeRAALAEERTE--GGTPLLIAARYGHLPVVHFLLeRCGANVALggsvnfdgET 80
Cdd:PLN03192 525 MASNLLTVASTGNAALLEELL-------KAKLDPDIGDskGRTPLHIAASKGYEDCVLVLL-KHACNVHI--------RD 588

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155   81 IEGAPPLWAASAAGHLPVVKaLLEHGAPVNNTTlTNSTPLRAACFDGHLEIVRYLVEHQADLEVANRHGHTCLMISCYKG 160
Cdd:PLN03192 589 ANGNTALWNAISAKHHKIFR-ILYHFASISDPH-AAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAED 666

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 41054155  161 HREIAQFLLEKGADVNRKSvkgntaLHDcaESGSLEIMKMLLK 203
Cdd:PLN03192 667 HVDMVRLLIMNGADVDKAN------TDD--DFSPTELRELLQK 701
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
476-572 1.04e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 59.97  E-value: 1.04e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155 476 LNPRARGGHTPLHMAVDRDttsvgrypvgrfpSLAVASLLLECGADVDSRDYDNNTPLHIAAANGCPDIMAALIRAGAHF 555
Cdd:COG0666 179 VNARDNDGETPLHLAAENG-------------HLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADL 245

                        90
                ....*....|....*..
gi 41054155 556 DATNAAQQTAYQLLEAQ 572
Cdd:COG0666 246 NAKDKDGLTALLLAAAA 262
Ank_4 pfam13637
Ankyrin repeats (many copies);
116-169 4.07e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.66  E-value: 4.07e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 41054155   116 NSTPLRAACFDGHLEIVRYLVEHQADLEVANRHGHTCLMISCYKGHREIAQFLL 169
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
85-136 1.44e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.12  E-value: 1.44e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 41054155    85 PPLWAASAAGHLPVVKALLEHGAPVNNTTLTNSTPLRAACFDGHLEIVRYLV 136
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 98-218 5.53e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 55.66  E-value: 5.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155   98 VVKALLEHGAPVNNTTL-TNSTPLRAACFDGHLEIVRYLVEHQADLEVANRHGHTCLMISCYKGHREIAQFLLEKGADVN 176
Cdd:PHA02878 149 ITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTD 228

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 41054155  177 RKSVKGNTALHdcAESGSL---EIMKMLLKCDARMERDGY--GMTPL 218
Cdd:PHA02878 229 ARDKCGNTPLH--ISVGYCkdyDILKLLLEHGVDVNAKSYilGLTAL 273
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 83-221 6.09e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 55.66  E-value: 6.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155   83 GAPPLWAASAAGHLPVVKALLEHGAPVNNTTLTNSTPLRAACFDGHLEIVRYLVEHQADLEVANRHGHTCLMISC-YKGH 161
Cdd:PHA02878 168 GNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVgYCKD 247

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41054155  162 REIAQFLLEKGADVNRKS-VKGNTALHDCAESGslEIMKMLLKCDARMER-DGYGMTPLLAA 221
Cdd:PHA02878 248 YDILKLLLEHGVDVNAKSyILGLTALHSSIKSE--RKLKLLLEYGADINSlNSYKLTPLSSA 307
PHA02798 PHA02798
ankyrin-like protein; Provisional
 96-187 7.05e-08

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 55.23  E-value: 7.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155   96 LPVVKALLEHGAPVNNTTLTNSTPLRAACFDGH---LEIVRYLVEHQADLEVANRHGHTCLMISCYKGHR---EIAQFLL 169
Cdd:PHA02798  89 LDIVKILIENGADINKKNSDGETPLYCLLSNGYinnLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLL 168

                         90
                 ....*....|....*....
gi 41054155  170 EKGADVNRKSVK-GNTALH 187
Cdd:PHA02798 169 EKGVDINTHNNKeKYDTLH 187
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 48-234 1.42e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 54.23  E-value: 1.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155   48 AARYGHLPVVHFLLErcganvaLGGSVNFdgETIEGAPPLWAASAAGHLPVVKALLEHGAPVNNTTLTNSTPLRAACFDG 127
Cdd:PHA02875   9 AILFGELDIARRLLD-------IGINPNF--EIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155  128 HLEIVRYLVEHQADL-EVANRHGHTCLMISCYKGHREIAQFLLEKGADVNRKSVKGNTALHDCAESGSLEIMKMLLKCDA 206
Cdd:PHA02875  80 DVKAVEELLDLGKFAdDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKA 159

                        170       180
                 ....*....|....*....|....*....
gi 41054155  207 RME-RDGYGMTPLLAASVTGHTNIVEFLV 234
Cdd:PHA02875 160 CLDiEDCCGCTPLIIAMAKGDIAICKMLL 188
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 91-169 1.44e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.52  E-value: 1.44e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41054155   91 SAAGHLPVVKALLEHGAPVNNTTLTNSTPLRAACFDGHLEIVRYLVEHQADLEVANRHGHTCLMISCYKGHREIAQFLL 169
Cdd:PTZ00322  90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
Ank_4 pfam13637
Ankyrin repeats (many copies);
149-202 1.54e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.04  E-value: 1.54e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 41054155   149 GHTCLMISCYKGHREIAQFLLEKGADVNRKSVKGNTALHDCAESGSLEIMKMLL 202
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02798 PHA02798
ankyrin-like protein; Provisional
 96-203 1.87e-07

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 54.07  E-value: 1.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155   96 LPVVKALLEHGAPVNNTTLTNSTPLraaC--------FDGHLEIVRYLVEHQADLEVANRHGHT---CLMISCYKGHREI 164
Cdd:PHA02798  51 TDIVKLFINLGANVNGLDNEYSTPL---CtilsnikdYKHMLDIVKILIENGADINKKNSDGETplyCLLSNGYINNLEI 127

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 41054155  165 AQFLLEKGADVNRKSVKGNTALHDCAESG---SLEIMKMLLK 203
Cdd:PHA02798 128 LLFMIENGADTTLLDKDGFTMLQVYLQSNhhiDIEIIKLLLE 169
Ank_2 pfam12796
Ankyrin repeats (3 copies);
469-559 3.21e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 48.57  E-value: 3.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155   469 TVYRLLKLNPRARG----GHTPLHMAVDRDttsvgrypvgrfpSLAVASLLLECgADVDSRDYdNNTPLHIAAANGCPDI 544
Cdd:pfam12796  12 LVKLLLENGADANLqdknGRTALHLAAKNG-------------HLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEI 76

                          90
                  ....*....|....*
gi 41054155   545 MAALIRAGAHFDATN 559
Cdd:pfam12796  77 VKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 476-560 1.00e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 51.56  E-value: 1.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155  476 LNPRARGGHTPLHMAVDRDTTsvgrypvgrfpsLAVASLLLECGADVDSRDYDNNTPLHIAAANGC--PDIMAALIRAGA 553
Cdd:PHA03095  76 VNAPERCGFTPLHLYLYNATT------------LDVIKLLIKAGADVNAKDKVGRTPLHVYLSGFNinPKVIRLLLRKGA 143


                 ....*..
gi 41054155  554 HFDATNA 560
Cdd:PHA03095 144 DVNALDL 150
Ank_5 pfam13857
Ankyrin repeats (many copies);
135-187 1.23e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.80  E-value: 1.23e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 41054155   135 LVEH-QADLEVANRHGHTCLMISCYKGHREIAQFLLEKGADVNRKSVKGNTALH 187
Cdd:pfam13857   1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 512-575 1.39e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.44  E-value: 1.39e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41054155  512 ASLLLECGADVDSRDYDNNTPLHIAAANGCPDIMAALIRAGAHFDATNAAQQTAYQLLEAQSSG 575
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFR 161
Ank_4 pfam13637
Ankyrin repeats (many copies);
182-234 1.74e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.34  E-value: 1.74e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 41054155   182 GNTALHDCAESGSLEIMKMLLKCDARM-ERDGYGMTPLLAASVTGHTNIVEFLV 234
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADInAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 132-204 2.02e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.05  E-value: 2.02e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41054155  132 VRYLVEHQADLEVANRHGHTCLMISCYKGHREIAQFLLEKGADVNRKSVKGNTALHDCAESGSLEIMKMLLKC 204
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PHA03095 PHA03095
ankyrin-like protein; Provisional
 129-550 2.10e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 50.41  E-value: 2.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155  129 LEIVRYLVEHQADLEVANRHG----HTCLMISCYKGhREIAQFLLEKGADVNRKSVKGNTALHDCAESGS-LEIMKMLLK 203
Cdd:PHA03095  27 VEEVRRLLAAGADVNFRGEYGktplHLYLHYSSEKV-KDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIK 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155  204 CDARM-ERDGYGMTPLLA--ASVTGHTNIVEFLVhqpraSREQRIHALELLGATFVDkkrdllgamrywrramelrwagg 280
Cdd:PHA03095 106 AGADVnAKDKVGRTPLHVylSGFNINPKVIRLLL-----RKGADVNALDLYGMTPLA----------------------- 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155  281 qagalekptagplvpAYDCSREVsTAEELEALI------TDPDDMRMQALlvrERILGPAHPDTSYyiryrgavyadsgn 354
Cdd:PHA03095 158 ---------------VLLKSRNA-NVELLRLLIdagadvYAVDDRFRSLL---HHHLQSFKPRARI-------------- 204

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155  355 FERCIRLWKYALDMQQSNLEPLSPMTASSFLSFAELFSFVlqdrAKGtlaarvsfqdlmgvlsksvreveravaqrerpp 434
Cdd:PHA03095 205 VRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVLPLL----IAG--------------------------------- 247

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155  435 eppqfskalsiilhllfllqklrcgpeqehlkrqtvyrlLKLNPRARGGHTPLHMAVDRDTTSVGRYpvgrfpslavasl 514
Cdd:PHA03095 248 ---------------------------------------ISINARNRYGQTPLHYAAVFNNPRACRR------------- 275

                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 41054155  515 LLECGADVDSRDYDNNTPLHIAAANGCPDIMAALIR 550
Cdd:PHA03095 276 LIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALA 311
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 86-202 3.15e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 49.88  E-value: 3.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155   86 PLWAASAAGHLPVVKALLEHGAPVNNTTLTNSTPLRAACFDGHLEIVRYLVE------------------HQADLEVANr 147
Cdd:PHA02878  40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRsinkcsvfytlvaikdafNNRNVEIFK- 118

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41054155  148 hghtCLMISCYKGHR------------------EIAQFLLEKGADVNRKSV-KGNTALHDCAESGSLEIMKMLL 202
Cdd:PHA02878 119 ----IILTNRYKNIQtidlvyidkkskddiieaEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLL 188
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 483-553 3.52e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 49.66  E-value: 3.52e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41054155  483 GHTPLHMAVDrdttsvgrypvgrFPSLAVASLLLECGADVDSRDYDNNTPLHIAAANGCPDIMAALIRAGA 553
Cdd:PHA03100 192 GFTPLHYAVY-------------NNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 87-234 8.19e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 49.10  E-value: 8.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155   87 LWAASAAGHLPVVKALLEHGAPVNNTTLTNSTPLRAACFDGHLEIVRYLVEHQADLEVANRHGHTCLMISCYKGHREIAQ 166
Cdd:PLN03192 529 LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFR 608

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41054155  167 FLLEKGADVNRKSvkGNTALHDCAESGSLEIMKMLLKCDARME-RDGYGMTPLLAASVTGHTNIVEFLV 234
Cdd:PLN03192 609 ILYHFASISDPHA--AGDLLCTAAKRNDLTAMKELLKQGLNVDsEDHQGATALQVAMAEDHVDMVRLLI 675
Ank_2 pfam12796
Ankyrin repeats (3 copies);
487-549 8.70e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 44.34  E-value: 8.70e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41054155   487 LHMAVdrdttsvgrypvgRFPSLAVASLLLECGADVDSRDYDNNTPLHIAAANGCPDIMAALI 549
Cdd:pfam12796   1 LHLAA-------------KNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL 50
Ank_5 pfam13857
Ankyrin repeats (many copies);
515-568 1.30e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.72  E-value: 1.30e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 41054155   515 LLECG-ADVDSRDYDNNTPLHIAAANGCPDIMAALIRAGAHFDATNAAQQTAYQL 568
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 41-200 1.38e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 47.74  E-value: 1.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155   41 GGTPLLIAARYGH--LPVVHFLLERcGANVALGGSVNF--------DGETIEGAPPLWAASAAGHLPVVKALLEHGAPVN 110
Cdd:PHA03100 141 GENLLHLYLESNKidLKILKLLIDK-GVDINAKNRVNYllsygvpiNIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPN 219

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155  111 NTTLTNSTPLRAACFDGHLEIVRYLVEHQADLEVANRH--------GHTCLMISCYKgHREIAQFLLEKGADVNRKSVKG 182
Cdd:PHA03100 220 LVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIETllyfkdkdLNTITKIKMLK-KSIMYMFLLDPGFYKNRKLIEN 298

                        170
                 ....*....|....*...
gi 41054155  183 NTALHDCAESGSLEIMKM 200
Cdd:PHA03100 299 SKSLKDVINECEKEIERM 316
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 477-557 1.60e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.97  E-value: 1.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155  477 NPRARGGHTPLHMAvdrdtTSVGRypvgrfpsLAVASLLLECGADVDSRDYDNNTPLHIAAANGCPDIMAALIR-AGAHF 555
Cdd:PTZ00322 109 NCRDYDGRTPLHIA-----CANGH--------VQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRhSQCHF 175


                 ..
gi 41054155  556 DA 557
Cdd:PTZ00322 176 EL 177
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
509-579 2.29e-05

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 46.49  E-value: 2.29e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41054155 509 LAVASLLLECGADVDSRDYDNNTPLHIAAANGCPDIMAALIRAGAHFDATNAAQQTAyqLLEAQSSGRHAL 579
Cdd:COG0666  67 LLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETP--LHLAAYNGNLEI 135
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 148-176 3.94e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 40.65  E-value: 3.94e-05
                           10        20
                   ....*....|....*....|....*....
gi 41054155    148 HGHTCLMISCYKGHREIAQFLLEKGADVN 176
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 66-222 4.64e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.60  E-value: 4.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155   66 ANVALGGSVNFDGETIEGAPPLWAASAAGHLPVVKALLEHGAPVNNTTLTNSTPLRAACFDGHLEIVRYLVEHQADLE-- 143
Cdd:PHA02876 161 AEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINkn 240

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155  144 -------VANRHGHTCLM----------ISCYKGH-----------REIAQFLLEKGADVNRKSVKGNTALHDCAESG-S 194
Cdd:PHA02876 241 dlsllkaIRNEDLETSLLlydagfsvnsIDDCKNTplhhasqapslSRLVPKLLERGADVNAKNIKGETPLYLMAKNGyD 320

                        170       180
                 ....*....|....*....|....*....
gi 41054155  195 LEIMKMLLKCDARME-RDGYGMTPLLAAS 222
Cdd:PHA02876 321 TENIRTLIMLGADVNaADRLYITPLHQAS 349
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 65-138 4.78e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.43  E-value: 4.78e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41054155   65 GANVALGGSVNFDGETIEGAPPLWAASAAGHLPVVKALLEHGAPVNNTTLTNSTPLRAACFDGHLEIVRYLVEH 138
Cdd:PTZ00322  97 GARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 148-178 1.40e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.19  E-value: 1.40e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 41054155   148 HGHTCLMISCYK-GHREIAQFLLEKGADVNRK 178
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNAR 32
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 129-235 1.90e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 44.27  E-value: 1.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155  129 LEIVRYLVEHQADLEVANRHGHTCLMIscYKGHREIA--QFLLEKGADVNRKSVKGNTALHDCAESGS-----LEIMKML 201
Cdd:PHA03100  15 VKNIKYIIMEDDLNDYSYKKPVLPLYL--AKEARNIDvvKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLL 92

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 41054155  202 LKCDARMER-DGYGMTPLLAASVT--GHTNIVEFLVH 235
Cdd:PHA03100  93 LEYGANVNApDNNGITPLLYAISKksNSYSIVEYLLD 129
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 37-221 2.06e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 44.21  E-value: 2.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155   37 ERTEGGTPLLIAARYGHLPVVHFLLERcganvalGGSVNFDGETIEGapPLWAASAAGHLPVVKALLEHGAPVNNTTLTN 116
Cdd:PHA02875  31 EIYDGISPIKLAMKFRDSEAIKLLMKH-------GAIPDVKYPDIES--ELHDAVEEGDVKAVEELLDLGKFADDVFYKD 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155  117 -STPLRAACFDGHLEIVRYLVEHQADLEVANRHGHTCLMISCYKGHREIAQFLLEKGADVNRKSVKGNTALHDCAESGSL 195
Cdd:PHA02875 102 gMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDI 181

                        170       180
                 ....*....|....*....|....*.
gi 41054155  196 EIMKMLLkcDARMERDGYGMTPLLAA 221
Cdd:PHA02875 182 AICKMLL--DSGANIDYFGKNGCVAA 205
Ank_4 pfam13637
Ankyrin repeats (many copies);
483-549 2.14e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.18  E-value: 2.14e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41054155   483 GHTPLHMAVdrdttsvgrypvgRFPSLAVASLLLECGADVDSRDYDNNTPLHIAAANGCPDIMAALI 549
Cdd:pfam13637   1 ELTALHAAA-------------ASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
102-151 2.58e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.25  E-value: 2.58e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 41054155   102 LLEHG-APVNNTTLTNSTPLRAACFDGHLEIVRYLVEHQADLEVANRHGHT 151
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLT 51
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 474-559 4.22e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 43.03  E-value: 4.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155  474 LKLNPRARGGHTPLHMAVDRDttsvgrypvgrfpSLAVASLLLECGADVDSRDYDNNTPLHIAAANGCPDIMAALIRAGA 553
Cdd:PHA02874 115 IDVNIKDAELKTFLHYAIKKG-------------DLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGA 181


                 ....*.
gi 41054155  554 HFDATN 559
Cdd:PHA02874 182 YANVKD 187
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 528-557 4.37e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 38.01  E-value: 4.37e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 41054155   528 DNNTPLHIAAANGCPDIMAALIRAGAHFDA 557
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 514-568 4.38e-04

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 41.02  E-value: 4.38e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 41054155  514 LLLECGADVDSRD-YDNNTPLHIAAANGCPDIMAALIR-AGAHFDATNAAQQTAYQL 568
Cdd:PHA02736  76 LLMEWGADINGKErVFGNTPLHIAVYTQNYELATWLCNqPGVNMEILNYAFKTPYYV 132
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 504-571 4.64e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 43.13  E-value: 4.64e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41054155  504 GRFPSLAVASLLlECGADVDSRDYDNNTPLHIAAANGC-PDIMAALIRAGAHFDATNAAQQtaYQLLEA 571
Cdd:PHA02876 418 GTNPYMSVKTLI-DRGANVNSKNKDLSTPLHYACKKNCkLDVIEMLLDNGADVNAINIQNQ--YPLLIA 483
Ank_4 pfam13637
Ankyrin repeats (many copies);
41-103 5.10e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.41  E-value: 5.10e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41054155    41 GGTPLLIAARYGHLPVVHFLLERcGANVALggsVNFDGETiegapPLWAASAAGHLPVVKALL 103
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEK-GADINA---VDGNGET-----ALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 483-564 5.64e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 42.95  E-value: 5.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155  483 GHTPLHMAVDRDTTSVGRYpvgrfpslavaslLLECGADVDSRDYDNNTPLHIAAANGCPDIMAALIRAGAHFDATNAAQ 562
Cdd:PHA02878 168 GNTALHYATENKDQRLTEL-------------LLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCG 234


                 ..
gi 41054155  563 QT 564
Cdd:PHA02878 235 NT 236
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 467-565 8.17e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 42.36  E-value: 8.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155  467 RQTVYRLLKLNPRARGGHTPLHMAVDRDttsvgrypvgRFPSLAVAslLLECGADVDSRDYDNNTPLHIAAANGCPDIMA 546
Cdd:PHA02876 325 RTLIMLGADVNAADRLYITPLHQASTLD----------RNKDIVIT--LLELGANVNARDYCDKTPIHYAAVRNNVVIIN 392

                         90
                 ....*....|....*....
gi 41054155  547 ALIRAGAHFDATNAAQQTA 565
Cdd:PHA02876 393 TLLDYGADIEALSQKIGTA 411
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 90-248 8.56e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 42.44  E-value: 8.56e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155  90 ASAAGHLPVVKALLEhgaPVNNTTLTNSTPLRAACFDGHLEivRYLvehQADLEVANRHGHTCLMISCYKGHREIAQFLL 169
Cdd:cd22194  90 ASDTGKTCLMKALLN---INENTKEIVRILLAFAEENGILD--RFI---NAEYTEEAYEGQTALNIAIERRQGDIVKLLI 161

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155 170 EKGADVNRKSvKGNTAlhdcaesgsleimkmllkcDARMERDGY--GMTPLLAASVTGHTNIVEFL---VHQPRASREQR 244
Cdd:cd22194 162 AKGADVNAHA-KGVFF-------------------NPKYKHEGFyfGETPLALAACTNQPEIVQLLmekESTDITSQDSR 221


                ....*...
gi 41054155 245 ----IHAL 248
Cdd:cd22194 222 gntvLHAL 229
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 148-176 8.61e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.85  E-value: 8.61e-04
                          10        20
                  ....*....|....*....|....*....
gi 41054155   148 HGHTCLMISCYKGHREIAQFLLEKGADVN 176
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 502-593 1.01e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 42.16  E-value: 1.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155  502 PVGRFPSLAVASL--------LLECGADVDSRDYDNNTPLHIAAANGCPDIMAALIRAGAHFDATNAAQQTAyqLLEAQS 573
Cdd:PLN03192 523 PNMASNLLTVASTgnaalleeLLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTA--LWNAIS 600

                         90       100       110
                 ....*....|....*....|....*....|.
gi 41054155  574 SGRHA----LHPLNHTT-------LQCLAAR 593
Cdd:PLN03192 601 AKHHKifriLYHFASISdphaagdLLCTAAK 631
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 10-200 1.12e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 41.87  E-value: 1.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155   10 AARDGKLKLMQKLLinkspEERAALAEERTEGGTPLLIAARYGHLPVVHFLLERCG-ANVAlggsvNFDGETiegapPLW 88
Cdd:PHA02874 131 AIKKGDLESIKMLF-----EYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAyANVK-----DNNGES-----PLH 195

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155   89 AASAAGHLPVVKALLEHG-------------------------------APVNNTTLTNSTPLRAAC-FDGHLEIVRYLV 136
Cdd:PHA02874 196 NAAEYGDYACIKLLIDHGnhimnkckngftplhnaiihnrsaiellinnASINDQDIDGSTPLHHAInPPCDIDIIDILL 275

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41054155  137 EHQADLEVANRHGHTCLMISCYKGHRE------IAQFLLEKGAD-------VNRKSVKGNTALHDCAESGSLEIMKM 200
Cdd:PHA02874 276 YHKADISIKDNKGENPIDTAFKYINKDpvikdiIANAVLIKEADklkdsdfLEHIEIKDNKEFSDFIKECNEEIEDM 352
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 528-559 1.44e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.50  E-value: 1.44e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 41054155   528 DNNTPLHIAAA-NGCPDIMAALIRAGAHFDATN 559
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 468-553 1.64e-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: 41.54  E-value: 1.64e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155 468 QTVYRLLK---LNPRARG--GHTPLHMAVDRDttsvgrypvgrfpSLAVASLLLECGAD-----VDSRDYDNNTPLHIAA 537
Cdd:cd22192  31 QAIKKLLKcpsCDLFQRGalGETALHVAALYD-------------NLEAAVVLMEAAPElvnepMTSDLYQGETALHIAV 97

                        90
                ....*....|....*.
gi 41054155 538 ANGCPDIMAALIRAGA 553
Cdd:cd22192  98 VNQNLNLVRELIARGA 113
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 168-267 2.18e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.01  E-value: 2.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155  168 LLEKGADVNRKSVKGNTALHDCAESGSLEIMKMLLK--CDARMeRDGYGMTPLLAASVTGHTNIVEFLVHQPRASREQRI 245
Cdd:PLN03192 544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKhaCNVHI-RDANGNTALWNAISAKHHKIFRILYHFASISDPHAA 622

                         90       100
                 ....*....|....*....|..
gi 41054155  246 HALELLGAtfvdkKRDLLGAMR 267
Cdd:PLN03192 623 GDLLCTAA-----KRNDLTAMK 639
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 477-564 2.27e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 41.02  E-value: 2.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155  477 NPRARGGHTPLHmavdrdttsvgrYPVGRFPSLAVASLLLECGADVDSRDYDNN-TPLHIAAANgcPDIMAALIRAGAHF 555
Cdd:PHA02878 228 DARDKCGNTPLH------------ISVGYCKDYDILKLLLEHGVDVNAKSYILGlTALHSSIKS--ERKLKLLLEYGADI 293


                 ....*....
gi 41054155  556 DATNAAQQT 564
Cdd:PHA02878 294 NSLNSYKLT 302
PHA02741 PHA02741
hypothetical protein; Provisional
 121-187 2.42e-03

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 39.26  E-value: 2.42e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41054155  121 RAACFDGHLEIVRYLVE--HQADLEVANRHGHTCLMISCYKGHR----EIAQFLLEKGADVN-RKSVKGNTALH 187
Cdd:PHA02741  30 RCGCFDIIARFTPFIRGdcHAAALNATDDAGQMCIHIAAEKHEAqlaaEIIDHLIELGADINaQEMLEGDTALH 103
PHA03095 PHA03095
ankyrin-like protein; Provisional
 474-579 2.42e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 40.78  E-value: 2.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155  474 LKLNPRARG--GHTPLHMAVDRdtTSVgrypvgrfpSLAVASLLLECGADVDSRDYDNNTPLHIAAANGCPD--IMAALI 549
Cdd:PHA03095 141 KGADVNALDlyGMTPLAVLLKS--RNA---------NVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRarIVRELI 209

                         90       100       110
                 ....*....|....*....|....*....|
gi 41054155  550 RAGAHFDATNAAQQTAYQLLEAQSSGRHAL 579
Cdd:PHA03095 210 RAGCDPAATDMLGNTPLHSMATGSSCKRSL 239
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 528-557 2.97e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.64  E-value: 2.97e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 41054155    528 DNNTPLHIAAANGCPDIMAALIRAGAHFDA 557
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
6-61 3.92e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 35.71  E-value: 3.92e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 41054155     6 AVFNAARDGKLKLMQKLLINKSPeeraaLAEERTEGGTPLLIAARYGHLPVVHFLL 61
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGAD-----INAVDGNGETALHFAASNGNVEVLKLLL 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 77-113 4.46e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.96  E-value: 4.46e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 41054155    77 DGETiegapPL-WAASAAGHLPVVKALLEHGAPVNNTT 113
Cdd:pfam00023   1 DGNT-----PLhLAAGRRGNLEIVKLLLSKGADVNARD 33
Ank_5 pfam13857
Ankyrin repeats (many copies);
168-218 5.21e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.40  E-value: 5.21e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 41054155   168 LLEKG-ADVNRKSVKGNTALHDCAESGSLEIMKMLLK--CDARMeRDGYGMTPL 218
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAygVDLNL-KDEEGLTAL 53
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 40-68 5.52e-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: 34.54  E-value: 5.52e-03
                          10        20
                  ....*....|....*....|....*....
gi 41054155    40 EGGTPLLIAARYGHLPVVHFLLErCGANV 68
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLE-NGADI 28
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 118-147 5.71e-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. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.96  E-value: 5.71e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 41054155   118 TPL-RAACFDGHLEIVRYLVEHQADLEVANR 147
Cdd:pfam00023   4 TPLhLAAGRRGNLEIVKLLLSKGADVNARDK 34
PHA02798 PHA02798
ankyrin-like protein; Provisional
 129-234 5.96e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 39.43  E-value: 5.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155  129 LEIVRYLVEHQADLEVANRHGHT--CLMISC---YKGHREIAQFLLEKGADVNRKSVKGNTALHDCAESG---SLEIMKM 200
Cdd:PHA02798  51 TDIVKLFINLGANVNGLDNEYSTplCTILSNikdYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGyinNLEILLF 130

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 41054155  201 LLKCDARME-RDGYGMTPLLAASVTGHT---NIVEFLV 234
Cdd:PHA02798 131 MIENGADTTlLDKDGFTMLQVYLQSNHHidiEIIKLLL 168
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 483-526 6.06e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.57  E-value: 6.06e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 41054155   483 GHTPLHMAVdrdttsvgrypvGRFPSLAVASLLLECGADVDSRD 526
Cdd:pfam00023   2 GNTPLHLAA------------GRRGNLEIVKLLLSKGADVNARD 33
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 146-201 6.13e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 37.93  E-value: 6.13e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054155  146 NRHGHTCLMISCYKGH---REIAQFLLEKGADVNRK-SVKGNTALHDCAESGSLEIMKML 201
Cdd:PHA02736  52 NRHGKQCVHIVSNPDKadpQEKLKLLMEWGADINGKeRVFGNTPLHIAVYTQNYELATWL 111
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 515-559 6.67e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 39.47  E-value: 6.67e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 41054155  515 LLECGADVDSRDYDNNTPLHIAAANGCPDIMAALIRAGAHFDATN 559
Cdd:PLN03192 641 LLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 181-206 6.78e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.49  E-value: 6.78e-03
                           10        20
                   ....*....|....*....|....*.
gi 41054155    181 KGNTALHDCAESGSLEIMKMLLKCDA 206
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 164-202 8.34e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 39.28  E-value: 8.34e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 41054155  164 IAQFLLEKGADVNRKSVKGNTALHDCAESGSLEIMKMLL 202
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLL 198
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH