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Conserved domains on  [gi|7296936|gb|AAF52209|]
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uncharacterized protein Dmel_CG9121, isoform A [Drosophila melanogaster]

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];
141-362 8.42e-44

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 158.19  E-value: 8.42e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936  141 DPHLYDADVATPLHYAAYWGHEECVRILLEHNAPINVLNNDGYAPLHLGA--GFAGVTELLIKHGALVNAKTlSDGKTAL 218
Cdd:COG0666  46 ALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAArnGDLEIVKLLLEAGADVNARD-KDGETPL 124

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936  219 HMAIESKCAESARLLLQTNININDTDDDGETPLMAAIACSMLDVAEELVKRGARINIQDKQNHTALQYAVRGRHTQMAKL 298
Cdd:COG0666 125 HLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKL 204

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7296936  299 LLERGARRLASQH----LLHLAVESNVKELVELLLQYGESLSVWNLKNFTPIMLAIHRGRHEMLEYLL 362
Cdd:COG0666 205 LLEAGADVNAKDNdgktALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLL 272
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
 517-573 1.12e-03

SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more generic proteins that comprise a large family of E3 ubiquitin protein ligases.


:

Pssm-ID: 462192  Cd Length: 39  Bit Score: 36.76  E-value: 1.12e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 7296936    517 QPRSLQSLARLEIRRSLLRCLQtrpevqerylptqersslgRIVDEFAIPATLKRYL 573
Cdd:pfam07525   1 TPRSLQHLCRLAIRRALGKRRL-------------------GAIDKLPLPPLLKDYL 38
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
141-362 8.42e-44

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 158.19  E-value: 8.42e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936  141 DPHLYDADVATPLHYAAYWGHEECVRILLEHNAPINVLNNDGYAPLHLGA--GFAGVTELLIKHGALVNAKTlSDGKTAL 218
Cdd:COG0666  46 ALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAArnGDLEIVKLLLEAGADVNARD-KDGETPL 124

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936  219 HMAIESKCAESARLLLQTNININDTDDDGETPLMAAIACSMLDVAEELVKRGARINIQDKQNHTALQYAVRGRHTQMAKL 298
Cdd:COG0666 125 HLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKL 204

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7296936  299 LLERGARRLASQH----LLHLAVESNVKELVELLLQYGESLSVWNLKNFTPIMLAIHRGRHEMLEYLL 362
Cdd:COG0666 205 LLEAGADVNAKDNdgktALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLL 272
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 140-304 2.91e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 93.58  E-value: 2.91e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936   140 HDPHLYDADVATPLHYAAYWGHE-----ECVRILLEHNAPINVLNNDGYAPLHLGA----GFAGVTELLIKHGALVNAKT 210
Cdd:PHA03100  59 ADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAIskksNSYSIVEYLLDNGANVNIKN 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936   211 lSDGKTALHMAIESKCAES--ARLLLQTNININ----------------DTDDDGETPLMAAIACSMLDVAEELVKRGAR 272
Cdd:PHA03100 139 -SDGENLLHLYLESNKIDLkiLKLLIDKGVDINaknrvnyllsygvpinIKDVYGFTPLHYAVYNNNPEFVKYLLDLGAN 217

                        170       180       190
                 ....*....|....*....|....*....|..
gi 7296936   273 INIQDKQNHTALQYAVRGRHTQMAKLLLERGA 304
Cdd:PHA03100 218 PNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249
Ank_2 pfam12796
Ankyrin repeats (3 copies);
153-244 2.28e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.16  E-value: 2.28e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936    153 LHYAAYWGHEECVRILLEHNAPINVLNNDGYAPLHL--GAGFAGVTELLIKHgalVNAKTLSDGKTALHMAIESKCAESA 230
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLaaKNGHLEIVKLLLEH---ADVNLKDNGRTALHYAARSGHLEIV 77

                          90
                  ....*....|....
gi 7296936    231 RLLLQTNININDTD 244
Cdd:pfam12796  78 KLLLEKGADINVKD 91
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 195-370 3.25e-07

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 53.55  E-value: 3.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936    195 VTELLIKHGALVnaktlSDGKTALHMAIESK---CAESARLLLQ------TNININDTDDD----GETPLMAAIACSMLD 261
Cdd:TIGR00870  68 LTELLLNLSCRG-----AVGDTLLHAISLEYvdaVEAILLHLLAafrksgPLELANDQYTSeftpGITALHLAAHRQNYE 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936    262 VAEELVKRGARINI-------QDKQNHTALQYavrGRH----------TQMAKLLLERGARRLA----SQHLLHLAVESN 320
Cdd:TIGR00870 143 IVKLLLERGASVPAracgdffVKSQGVDSFYH---GESplnaaaclgsPSIVALLSEDPADILTadslGNTLLHLLVMEN 219

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7296936    321 V-----KELV----ELLLQYGESLS-------VWNLKNFTPIMLAIHRGRHEMLEYLLNVAEEQRK 370
Cdd:TIGR00870 220 EfkaeyEELScqmyNFALSLLDKLRdskelevILNHQGLTPLKLAAKEGRIVLFRLKLAIKYKQKK 285
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 151-177 2.82e-06

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: 44.12  E-value: 2.82e-06
                           10        20
                   ....*....|....*....|....*..
gi 7296936     151 TPLHYAAYWGHEECVRILLEHNAPINV 177
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 214-363 3.29e-06

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 50.01  E-value: 3.29e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936  214 GKTALHMAIESKCAESARLLLQ---TNININDTDD--DGETPLMAAIACSMLDVAEELVKRGAriniqDKQNHTA----- 283
Cdd:cd22192  51 GETALHVAALYDNLEAAVVLMEaapELVNEPMTSDlyQGETALHIAVVNQNLNLVRELIARGA-----DVVSPRAtgtff 125

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936  284 --------------LQYAVRGRHTQMAKLLLERGARRLASQHL----LH-LAVESN---VKELVELLLQY---GESLSVW 338
Cdd:cd22192 126 rpgpknliyygehpLSFAACVGNEEIVRLLIEHGADIRAQDSLgntvLHiLVLQPNktfACQMYDLILSYdkeDDLQPLD 205

                       170       180
                ....*....|....*....|....*...
gi 7296936  339 NLKN---FTPIMLAIHRGRHEMLEYLLN 363
Cdd:cd22192 206 LVPNnqgLTPFKLAAKEGNIVMFQHLVQ 233
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
 517-573 1.12e-03

SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more generic proteins that comprise a large family of E3 ubiquitin protein ligases.


Pssm-ID: 462192  Cd Length: 39  Bit Score: 36.76  E-value: 1.12e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 7296936    517 QPRSLQSLARLEIRRSLLRCLQtrpevqerylptqersslgRIVDEFAIPATLKRYL 573
Cdd:pfam07525   1 TPRSLQHLCRLAIRRALGKRRL-------------------GAIDKLPLPPLLKDYL 38
SOCS_ASB_like cd03716
SOCS (suppressors of cytokine signaling) box of ASB (ankyrin repeat and SOCS box) and SSB ...
 517-573 4.01e-03

SOCS (suppressors of cytokine signaling) box of ASB (ankyrin repeat and SOCS box) and SSB (SPRY domain-containing SOCS box proteins) protein families. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence of a variable number of repeats. SSB proteins contain a central SPRY domain and a C-terminal SOCS. Recently, it has been shown that all four SSB proteins interact with the MET, the receptor protein-tyrosine kinase for hepatocyte growth factor (HGF), and that SSB-1, SSB-2, and SSB-4 interact with prostate apoptosis response protein-4. Both types of interactions are mediated through the SPRY domain.


Pssm-ID: 239686  Cd Length: 42  Bit Score: 35.55  E-value: 4.01e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 7296936  517 QPRSLQSLARLEIRrsllRCLQTRPEVQerylptqersslgriVDEFAIPATLKRYL 573
Cdd:cd03716   2 TPRSLQHLCRLAIR----RCLGRRRLEL---------------IKKLPLPPRLKDYL 39
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
141-362 8.42e-44

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 158.19  E-value: 8.42e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936  141 DPHLYDADVATPLHYAAYWGHEECVRILLEHNAPINVLNNDGYAPLHLGA--GFAGVTELLIKHGALVNAKTlSDGKTAL 218
Cdd:COG0666  46 ALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAArnGDLEIVKLLLEAGADVNARD-KDGETPL 124

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936  219 HMAIESKCAESARLLLQTNININDTDDDGETPLMAAIACSMLDVAEELVKRGARINIQDKQNHTALQYAVRGRHTQMAKL 298
Cdd:COG0666 125 HLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKL 204

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7296936  299 LLERGARRLASQH----LLHLAVESNVKELVELLLQYGESLSVWNLKNFTPIMLAIHRGRHEMLEYLL 362
Cdd:COG0666 205 LLEAGADVNAKDNdgktALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLL 272
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
144-363 1.63e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 143.56  E-value: 1.63e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936  144 LYDADVATPLHYAAYWGHEECVRILLEHNAPINVLNNDGYAPLHL--GAGFAGVTELLIKHGALVNAKTlSDGKTALHMA 221
Cdd:COG0666  16 LLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAaaLAGDLLVALLLLAAGADINAKD-DGGNTLLHAA 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936  222 IESKCAESARLLLQTNININDTDDDGETPLMAAIACSMLDVAEELVKRGARINIQDKQNHTALQYAVRGRHTQMAKLLLE 301
Cdd:COG0666  95 ARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLE 174

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7296936  302 RGA----RRLASQHLLHLAVESNVKELVELLLQYGESLSVWNLKNFTPIMLAIHRGRHEMLEYLLN 363
Cdd:COG0666 175 AGAdvnaRDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
141-316 1.63e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 140.86  E-value: 1.63e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936  141 DPHLYDADVATPLHYAAYWGHEECVRILLEHNAPINVLNNDGYAPLHLGA--GFAGVTELLIKHGALVNAKTlSDGKTAL 218
Cdd:COG0666 112 DVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAanGNLEIVKLLLEAGADVNARD-NDGETPL 190

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936  219 HMAIESKCAESARLLLQTNININDTDDDGETPLMAAIACSMLDVAEELVKRGARINIQDKQNHTALQYAVRGRHTQMAKL 298
Cdd:COG0666 191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270

                       170
                ....*....|....*...
gi 7296936  299 LLERGARRLASQHLLHLA 316
Cdd:COG0666 271 LLLALLLLAAALLDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
167-363 8.73e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 124.68  E-value: 8.73e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936  167 ILLEHNAPINVLNNDGYAPLHLGAGFAGVTELLIKHGALVNAKTLSDGKTALHMAIESKCAESARLLLQTNININDTDDD 246
Cdd:COG0666   7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936  247 GETPLMAAIACSMLDVAEELVKRGARINIQDKQNHTALQYAVRGRHTQMAKLLLERGA----RRLASQHLLHLAVESNVK 322
Cdd:COG0666  87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGAdvnaQDNDGNTPLHLAAANGNL 166

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 7296936  323 ELVELLLQYGESLSVWNLKNFTPIMLAIHRGRHEMLEYLLN 363
Cdd:COG0666 167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLE 207
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
141-284 1.46e-27

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 112.74  E-value: 1.46e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936  141 DPHLYDADVATPLHYAAYWGHEECVRILLEHNAPINVLNNDGYAPLHLGA--GFAGVTELLIKHGALVNAKTlSDGKTAL 218
Cdd:COG0666 145 DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAenGHLEIVKLLLEAGADVNAKD-NDGKTAL 223

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7296936  219 HMAIESKCAESARLLLQTNININDTDDDGETPLMAAIACSMLDVAEELVKRGARINIQDKQNHTAL 284
Cdd:COG0666 224 DLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
198-363 1.40e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 92.32  E-value: 1.40e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936  198 LLIKHGALVNAKTLSDGKTALHMAIESKCAESARLLLQTNININDTDDDGETPLMAAIACSMLDVAEELVKRGARINIQD 277
Cdd:COG0666   5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936  278 KQNHTALQYAVRGRHTQMAKLLLERGA----RRLASQHLLHLAVESNVKELVELLLQYGESLSVWNLKNFTPIMLAIHRG 353
Cdd:COG0666  85 DGGNTLLHAAARNGDLEIVKLLLEAGAdvnaRDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANG 164

                       170
                ....*....|
gi 7296936  354 RHEMLEYLLN 363
Cdd:COG0666 165 NLEIVKLLLE 174
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 140-304 2.91e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 93.58  E-value: 2.91e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936   140 HDPHLYDADVATPLHYAAYWGHE-----ECVRILLEHNAPINVLNNDGYAPLHLGA----GFAGVTELLIKHGALVNAKT 210
Cdd:PHA03100  59 ADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAIskksNSYSIVEYLLDNGANVNIKN 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936   211 lSDGKTALHMAIESKCAES--ARLLLQTNININ----------------DTDDDGETPLMAAIACSMLDVAEELVKRGAR 272
Cdd:PHA03100 139 -SDGENLLHLYLESNKIDLkiLKLLIDKGVDINaknrvnyllsygvpinIKDVYGFTPLHYAVYNNNPEFVKYLLDLGAN 217

                        170       180       190
                 ....*....|....*....|....*....|..
gi 7296936   273 INIQDKQNHTALQYAVRGRHTQMAKLLLERGA 304
Cdd:PHA03100 218 PNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 153-363 1.00e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 92.04  E-value: 1.00e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936   153 LHYAAYWGHEECVRILLEHNAPINVLNNDG-----YAPLHLG--AGFAGVTELLIKHGALVNAKTLSDgKTALH-----M 220
Cdd:PHA03100   1 LYSYIVLTKSRIIKVKNIKYIIMEDDLNDYsykkpVLPLYLAkeARNIDVVKILLDNGADINSSTKNN-STPLHylsniK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936   221 AIESKCAESARLLLQTNININDTDDDGETPLMAAIACSM--LDVAEELVKRGARINIQDKQNHTALQYAVRGRH--TQMA 296
Cdd:PHA03100  80 YNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKKSnsYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKIL 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7296936   297 KLLLERGarrlasqhllhlaVESNVKELVELLLQYGESLSVWNLKNFTPIMLAIHRGRHEMLEYLLN 363
Cdd:PHA03100 160 KLLIDKG-------------VDINAKNRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLD 213
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 193-350 1.98e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 88.40  E-value: 1.98e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936   193 AGVTELLIKHGALVNAKTLSDGKTALHMAIESKCAESARLLLQTNININDTDDDGETPLMAAIACSMLDVAEELVKRGAR 272
Cdd:PHA02878 147 AEITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS 226

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936   273 INIQDKQNHTALQYAV-RGRHTQMAKLLLERGARRLASQHL-----LHLAVESNVKelVELLLQYGESLSVWNLKNFTPI 346
Cdd:PHA02878 227 TDARDKCGNTPLHISVgYCKDYDILKLLLEHGVDVNAKSYIlgltaLHSSIKSERK--LKLLLEYGADINSLNSYKLTPL 304


                 ....
gi 7296936   347 MLAI 350
Cdd:PHA02878 305 SSAV 308
Ank_2 pfam12796
Ankyrin repeats (3 copies);
153-244 2.28e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.16  E-value: 2.28e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936    153 LHYAAYWGHEECVRILLEHNAPINVLNNDGYAPLHL--GAGFAGVTELLIKHgalVNAKTLSDGKTALHMAIESKCAESA 230
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLaaKNGHLEIVKLLLEH---ADVNLKDNGRTALHYAARSGHLEIV 77

                          90
                  ....*....|....
gi 7296936    231 RLLLQTNININDTD 244
Cdd:pfam12796  78 KLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
218-304 1.62e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.77  E-value: 1.62e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936    218 LHMAIESKCAESARLLLQTNININDTDDDGETPLMAAIACSMLDVAEELVKRgARINIQDkQNHTALQYAVRGRHTQMAK 297
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78


                  ....*..
gi 7296936    298 LLLERGA 304
Cdd:pfam12796  79 LLLEKGA 85
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 151-279 6.00e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 80.48  E-value: 6.00e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936   151 TPLHYAAYW--GHEECVRILLEHNAPINVLNNDGYAPLHLGAGFAGVT----ELLIKHGALVNAKTLSD----------- 213
Cdd:PHA03100 108 TPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkilKLLIDKGVDINAKNRVNyllsygvpini 187

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936   214 ----GKTALHMAIESKCAESARLLLQTNININDTDDDGETPLMAAIACSMLDVAEELVKRGARINIQDKQ 279
Cdd:PHA03100 188 kdvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
PHA03095 PHA03095
ankyrin-like protein; Provisional
 145-363 2.60e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 78.53  E-value: 2.60e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936   145 YDADVA-------TPLHYAAYWGHEEC---VRILLEHNAPINVLNNDGYAPLHLGAGFA---GVTELLIKHGALVNAKTL 211
Cdd:PHA03095  36 AGADVNfrgeygkTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLHLYLYNAttlDVIKLLIKAGADVNAKDK 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936   212 SdGKTALHMAIESKC--AESARLLLQTNININDTDDDGETP-----------------LMAAIAC---------SMLD-- 261
Cdd:PHA03095 116 V-GRTPLHVYLSGFNinPKVIRLLLRKGADVNALDLYGMTPlavllksrnanvellrlLIDAGADvyavddrfrSLLHhh 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936   262 ---------VAEELVKRGARINIQDKQNHTALQYAVRG---RHTQMAKLLlERG----ARRLASQHLLHLAVESNVKELV 325
Cdd:PHA03095 195 lqsfkprarIVRELIRAGCDPAATDMLGNTPLHSMATGsscKRSLVLPLL-IAGisinARNRYGQTPLHYAAVFNNPRAC 273

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 7296936   326 ELLLQYGESLSVWNLKNFTPIMLAIHRGRHEMLEYLLN 363
Cdd:PHA03095 274 RRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALA 311
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 141-363 8.35e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 76.57  E-value: 8.35e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936   141 DPHLYDADVATPLHYAAYWGHEECVRILLEHNAPINVLNNDGYAPLH--LGAGFAGVTELLIKHGALVNAKTLSDGKTAL 218
Cdd:PHA02875  27 NPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHdaVEEGDVKAVEELLDLGKFADDVFYKDGMTPL 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936   219 HMAIESKCAESARLLLQTNININDTDDDGETPLMAAIACSMLDVAEELVKRGARINIQDKQNHTALQYAVRGRHTQMAKL 298
Cdd:PHA02875 107 HLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKM 186

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936   299 LLERGAR-----RLASQHLLHLAVESNVKELVELLLQYGESLSvwnlknftpIMLAIHRGRHEMLEYLLN 363
Cdd:PHA02875 187 LLDSGANidyfgKNGCVAALCYAIENNKIDIVRLFIKRGADCN---------IMFMIEGEECTILDMICN 247
Ank_2 pfam12796
Ankyrin repeats (3 copies);
251-337 1.11e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 69.76  E-value: 1.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936    251 LMAAIACSMLDVAEELVKRGARINIQDKQNHTALQYAVRGRHTQMAKLLLERGARRLASQHL--LHLAVESNVKELVELL 328
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRtaLHYAARSGHLEIVKLL 80


                  ....*....
gi 7296936    329 LQYGESLSV 337
Cdd:pfam12796  81 LEKGADINV 89
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 144-369 4.38e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 75.49  E-value: 4.38e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936   144 LYDADVA---------TPLHYAAYWGH-EECVRILLEHNAPINVLNNDGYAPLHLGAGFAGVTE---LLIKHGALVNAkT 210
Cdd:PHA02876 259 LYDAGFSvnsiddcknTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYDTEnirTLIMLGADVNA-A 337

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936   211 LSDGKTALHMAIE-SKCAESARLLLQTNININDTDDDGETPLMAAIACSMLDVAEELVKRGARINIQDKQNHTALQYAVR 289
Cdd:PHA02876 338 DRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALC 417

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936   290 GRHTQMA-KLLLERGAR-RLASQHL---LHLAVESNVK-ELVELLLQYGESLSVWNLKNFTPIMLAIhrGRHEMLEYLLN 363
Cdd:PHA02876 418 GTNPYMSvKTLIDRGANvNSKNKDLstpLHYACKKNCKlDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLH 495


                 ....*.
gi 7296936   364 VAEEQR 369
Cdd:PHA02876 496 YGAELR 501
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 151-255 6.69e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 71.06  E-value: 6.69e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936   151 TPLHYAAYWGHEECVRILLEHNAPINVLNNDGYAPLHLGAGFA---GVTELLIKHGALVNAKTLSDGKTALHMAIESKca 227
Cdd:PHA02878 203 SPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCkdyDILKLLLEHGVDVNAKSYILGLTALHSSIKSE-- 280

                         90       100
                 ....*....|....*....|....*...
gi 7296936   228 ESARLLLQTNININDTDDDGETPLMAAI 255
Cdd:PHA02878 281 RKLKLLLEYGADINSLNSYKLTPLSSAV 308
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 151-371 2.15e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 70.09  E-value: 2.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936   151 TPLHYAAYWGHEECVRILLEHNAPINVLNNDGYAPLHLGAGFAGVTEL--LIKHGALVNAKTLSdgktaLHMAIESKCAE 228
Cdd:PHA02876 180 TPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIkaIIDNRSNINKNDLS-----LLKAIRNEDLE 254

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936   229 SARLLLQTNININDTDDDGETPLMAAI-ACSMLDVAEELVKRGARINIQDKQNHTALQ-YAVRGRHTQMAKLLLERGARR 306
Cdd:PHA02876 255 TSLLLYDAGFSVNSIDDCKNTPLHHASqAPSLSRLVPKLLERGADVNAKNIKGETPLYlMAKNGYDTENIRTLIMLGADV 334

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936   307 LASQHL----LHLAVE-SNVKELVELLLQYGESLSVWNLKNFTPIMLAIHRGRHEMLEYLLNVAEEQRKL 371
Cdd:PHA02876 335 NAADRLyitpLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEAL 404
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 141-289 2.22e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 69.22  E-value: 2.22e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936   141 DPHLYDADVATPLHYAAYWGHEECVRILLEHNAPINVLNNDGYAPLHLG--AGFAGVTELLIKHGALVNAKTlSDGKTAL 218
Cdd:PHA02874 116 DVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAikHNFFDIIKLLLEKGAYANVKD-NNGESPL 194

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7296936   219 HMAIESKCAESARLLLQTNININDTDDDGETPLMAAIACSMLDVaeELVKRGARINIQDKQNHTALQYAVR 289
Cdd:PHA02874 195 HNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAI--ELLINNASINDQDIDGSTPLHHAIN 263
PHA03095 PHA03095
ankyrin-like protein; Provisional
 151-302 4.20e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 65.43  E-value: 4.20e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936   151 TPLH-YAA-YWGHEECVRILLEHNAPINVLNNDGYAPLHLGAGFAGVT----ELLIKHGA----------------LVNA 208
Cdd:PHA03095 119 TPLHvYLSgFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANvellRLLIDAGAdvyavddrfrsllhhhLQSF 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936   209 K------------------TLSDGKTALH-MAIESKCAESARL-LLQTNININDTDDDGETPLMAAiACSMLDVA-EELV 267
Cdd:PHA03095 199 KprarivreliragcdpaaTDMLGNTPLHsMATGSSCKRSLVLpLLIAGISINARNRYGQTPLHYA-AVFNNPRAcRRLI 277

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 7296936   268 KRGARINIQDKQNHTALQYAVRGRHTQMAKLLLER 302
Cdd:PHA03095 278 ALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAK 312
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 146-278 1.20e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 63.83  E-value: 1.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936   146 DADVATPLHYAAYWGHEECVRILLEHNAPINVLNNDGYAPLHLGAGF-AGVTELLIKHgALVNAKTLsDGKTALHMAIES 224
Cdd:PHA02874 187 DNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHnRSAIELLINN-ASINDQDI-DGSTPLHHAINP 264

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 7296936   225 KCA-ESARLLLQTNININDTDDDGETPLMAAIA-CSMLDVAEELVKRGARINIQDK 278
Cdd:PHA02874 265 PCDiDIIDILLYHKADISIKDNKGENPIDTAFKyINKDPVIKDIIANAVLIKEADK 320
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 148-351 1.37e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 63.83  E-value: 1.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936   148 DVATPLHYAAYWGHEECVRILLEHNAPINVLNNDGYAPL--HLGAGFAGVTELLIKHGA--------------------- 204
Cdd:PHA02874  34 ETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLltAIKIGAHDIIKLLIDNGVdtsilpipciekdmiktildc 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936   205 --LVNAKTlSDGKTALHMAIESKCAESARLLLQTNININDTDDDGETPLMAAIACSMLDVAEELVKRGARINIQDKQNHT 282
Cdd:PHA02874 114 giDVNIKD-AELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGES 192

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7296936   283 ALQYAVRGRHTQMAKLLLERGARRLASQHL----LHLAVESNvKELVELLLQyGESLSVWNLKNFTPIMLAIH 351
Cdd:PHA02874 193 PLHNAAEYGDYACIKLLIDHGNHIMNKCKNgftpLHNAIIHN-RSAIELLIN-NASINDQDIDGSTPLHHAIN 263
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 190-363 1.55e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 63.44  E-value: 1.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936   190 AGFAGVTELLIKHGALVNAKTlSDGKTALHMAIESKCAESARLLLqtninindtdDDGETPLMAAIACSMLDVAEELVKR 269
Cdd:PHA02874  45 SGDAKIVELFIKHGADINHIN-TKIPHPLLTAIKIGAHDIIKLLI----------DNGVDTSILPIPCIEKDMIKTILDC 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936   270 GARINIQDKQNHTALQYAVRGRHTQMAKLLLERGA----RRLASQHLLHLAVESNVKELVELLLQYGESLSVWNLKNFTP 345
Cdd:PHA02874 114 GIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGAdvniEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESP 193

                        170
                 ....*....|....*...
gi 7296936   346 IMLAIHRGRHEMLEYLLN 363
Cdd:PHA02874 194 LHNAAEYGDYACIKLLID 211
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 141-304 1.95e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 63.73  E-value: 1.95e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936   141 DPHLYDADVATPLHYAAYWGHEECVRILLEHNAPINVLNndgyaplhlgagfagvtellikhgalvnaktlSDGKTALHM 220
Cdd:PLN03192 550 DPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRD--------------------------------ANGNTALWN 597

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936   221 AIESKCAESARLLLQTNiNINDTDDDGETPLMAAIAcSMLDVAEELVKRGARINIQDKQNHTALQYAVRGRHTQMAKLLL 300
Cdd:PLN03192 598 AISAKHHKIFRILYHFA-SISDPHAAGDLLCTAAKR-NDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLI 675


                 ....
gi 7296936   301 ERGA 304
Cdd:PLN03192 676 MNGA 679
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 152-380 4.87e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 58.74  E-value: 4.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936   152 PLHYAAYWGHEECVRILLEHNAPINVLNNDGYAPLHL---GAGFAGVTELLikhgALVNAKTLSDGKTALHMAIESKCAE 228
Cdd:PHA02878  40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIickEPNKLGMKEMI----RSINKCSVFYTLVAIKDAFNNRNVE 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936   229 SARLLLQTNININDTDDDGETPLMAAIACSMLDVAEELVKRGARINIQDK-QNHTALQYAVRGRHTQMAKLLLERGAR-- 305
Cdd:PHA02878 116 IFKIILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANvn 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936   306 --RLASQHLLHLAVESNVKELVELLLQYGESLSVWNLKNFTPIMLAIHRGR-HEMLEYLL------NVAEEQRKL-GLYS 375
Cdd:PHA02878 196 ipDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKdYDILKLLLehgvdvNAKSYILGLtALHS 275


                 ....*
gi 7296936   376 DVHDE 380
Cdd:PHA02878 276 SIKSE 280
PHA03095 PHA03095
ankyrin-like protein; Provisional
 141-241 9.51e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 58.11  E-value: 9.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936   141 DPHLYDADVATPLHYAAYwgHEECVRI----LLEHNAPINVLNNDGYAPLHLGAGF--AGVTELLIKHGALVNAKTlSDG 214
Cdd:PHA03095 214 DPAATDMLGNTPLHSMAT--GSSCKRSlvlpLLIAGISINARNRYGQTPLHYAAVFnnPRACRRLIALGADINAVS-SDG 290

                         90       100
                 ....*....|....*....|....*..
gi 7296936   215 KTALHMAIESKCAESARLLLQTNININ 241
Cdd:PHA03095 291 NTPLSLMVRNNNGRAVRAALAKNPSAE 317
Ank_2 pfam12796
Ankyrin repeats (3 copies);
313-365 1.87e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 52.04  E-value: 1.87e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 7296936    313 LHLAVESNVKELVELLLQYGESLSVWNLKNFTPIMLAIHRGRHEMLEYLLNVA 365
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA 53
Ank_4 pfam13637
Ankyrin repeats (many copies);
151-200 2.22e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.74  E-value: 2.22e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 7296936    151 TPLHYAAYWGHEECVRILLEHNAPINVLNNDGYAPLHLGA--GFAGVTELLI 200
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAAsnGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
232-287 8.84e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.88  E-value: 8.84e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 7296936    232 LLLQTNININDTDDDGETPLMAAIACSMLDVAEELVKRGARINIQDKQNHTALQYA 287
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 218-379 2.67e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.43  E-value: 2.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936   218 LHMAIESKCAESARLLLQTNIN-INDTDDDGETPLMAAIACSMLDVAEELVKRGARINIQDKQNHTALQYAVRGRHTQMA 296
Cdd:PHA02874   5 LRMCIYSGDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDII 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936   297 KLLLERGA---------------------------RRLASQHLLHLAVESNVKELVELLLQYGESLSVWNLKNFTPIMLA 349
Cdd:PHA02874  85 KLLIDNGVdtsilpipciekdmiktildcgidvniKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIA 164

                        170       180       190
                 ....*....|....*....|....*....|
gi 7296936   350 IHRGRHEMLEYLLnvaeeqrKLGLYSDVHD 379
Cdd:PHA02874 165 IKHNFFDIIKLLL-------EKGAYANVKD 187
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 195-370 3.25e-07

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 53.55  E-value: 3.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936    195 VTELLIKHGALVnaktlSDGKTALHMAIESK---CAESARLLLQ------TNININDTDDD----GETPLMAAIACSMLD 261
Cdd:TIGR00870  68 LTELLLNLSCRG-----AVGDTLLHAISLEYvdaVEAILLHLLAafrksgPLELANDQYTSeftpGITALHLAAHRQNYE 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936    262 VAEELVKRGARINI-------QDKQNHTALQYavrGRH----------TQMAKLLLERGARRLA----SQHLLHLAVESN 320
Cdd:TIGR00870 143 IVKLLLERGASVPAracgdffVKSQGVDSFYH---GESplnaaaclgsPSIVALLSEDPADILTadslGNTLLHLLVMEN 219

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7296936    321 V-----KELV----ELLLQYGESLS-------VWNLKNFTPIMLAIHRGRHEMLEYLLNVAEEQRK 370
Cdd:TIGR00870 220 EfkaeyEELScqmyNFALSLLDKLRdskelevILNHQGLTPLKLAAKEGRIVLFRLKLAIKYKQKK 285
PHA03095 PHA03095
ankyrin-like protein; Provisional
 226-485 3.30e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 53.10  E-value: 3.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936   226 CAESARLLLQTNININDTDDDGETPLMAAIACSMLDVAEE---LVKRGARINIQDKQNHTALQYAVRGRHT-QMAKLLLE 301
Cdd:PHA03095  26 TVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIK 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936   302 RGARRLAS----QHLLH--LAVESNVKELVELLLQYGESLSVWNLKNFTP--IMLAIHRGRHEMLEYLLNVAEEQRklgl 373
Cdd:PHA03095 106 AGADVNAKdkvgRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPlaVLLKSRNANVELLRLLIDAGADVY---- 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936   374 ysDVHDEGLVLFAVQQNFwVKEFSRILRVLLAK--SPSARNDF----------YDSCAPTIVCGLI-----------YCH 430
Cdd:PHA03095 182 --AVDDRFRSLLHHHLQS-FKPRARIVRELIRAgcDPAATDMLgntplhsmatGSSCKRSLVLPLLiagisinarnrYGQ 258

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 7296936   431 TPLSRAINLHRLEVAEFLIHEGCNLAqicrehvvneLRSNCTPTRLAFARLLCNA 485
Cdd:PHA03095 259 TPLHYAAVFNNPRACRRLIALGADIN----------AVSSDGNTPLSLMVRNNNG 303
Ank_4 pfam13637
Ankyrin repeats (many copies);
311-362 6.09e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.50  E-value: 6.09e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 7296936    311 HLLHLAVESNVKELVELLLQYGESLSVWNLKNFTPIMLAIHRGRHEMLEYLL 362
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02798 PHA02798
ankyrin-like protein; Provisional
 146-363 6.53e-07

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 52.14  E-value: 6.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936   146 DADVATPL-----HYAAYWGHEECVRILLEHNAPINVLNNDGYAPLH--LGAGFAGVTELL---IKHGALVNAKTlSDGK 215
Cdd:PHA02798  68 DNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYclLSNGYINNLEILlfmIENGADTTLLD-KDGF 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936   216 TALHMAIESKCA---ESARLLLQTNININD-TDDDGETPL----MAAIACSMLDVAEELVKRGARINIQDKQNHtalqya 287
Cdd:PHA02798 147 TMLQVYLQSNHHidiEIIKLLLEKGVDINThNNKEKYDTLhcyfKYNIDRIDADILKLFVDNGFIINKENKSHK------ 220

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7296936   288 vrgrhtqmaKLLLErgarRLASQHLLHLAVESNVkelVELLLQYGEsLSVWNLKNFTPIMLAIHRGRHEMLEYLLN 363
Cdd:PHA02798 221 ---------KKFME----YLNSLLYDNKRFKKNI---LDFIFSYID-INQVDELGFNPLYYSVSHNNRKIFEYLLQ 279
Ank_4 pfam13637
Ankyrin repeats (many copies);
216-267 8.02e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.11  E-value: 8.02e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 7296936    216 TALHMAIESKCAESARLLLQTNININDTDDDGETPLMAAIACSMLDVAEELV 267
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
249-300 1.44e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.34  E-value: 1.44e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 7296936    249 TPLMAAIACSMLDVAEELVKRGARINIQDKQNHTALQYAVRGRHTQMAKLLL 300
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 195-353 1.92e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 50.83  E-value: 1.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936   195 VTELLIKHGALVNAKTLSdGKTALHMAIESKCAESARLLLQTNININDTDDDGETPLMAAIACSMLDVAEELVKRGARIN 274
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIY-CITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNIN 238

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936   275 iqdkQNHTALQYAVRGRHTQMAKLLLERG----ARRLASQHLLHLAVES-NVKELVELLLQYGESLSVWNLKNFTPIMLA 349
Cdd:PHA02876 239 ----KNDLSLLKAIRNEDLETSLLLYDAGfsvnSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIKGETPLYLM 314


                 ....
gi 7296936   350 IHRG 353
Cdd:PHA02876 315 AKNG 318
PHA02798 PHA02798
ankyrin-like protein; Provisional
 195-303 1.98e-06

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 50.60  E-value: 1.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936   195 VTELLIKHGALVNAK----------TLSDGKTALHMaieskcAESARLLLQTNININDTDDDGETPLMAAIACSMLDVAE 264
Cdd:PHA02798  53 IVKLFINLGANVNGLdneystplctILSNIKDYKHM------LDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLE 126

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 7296936   265 EL---VKRGARINIQDKQNHTALQYAVRGRHT---QMAKLLLERG 303
Cdd:PHA02798 127 ILlfmIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKG 171
Ank_5 pfam13857
Ankyrin repeats (many copies);
135-188 2.73e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.64  E-value: 2.73e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 7296936    135 VSCREHDPHLYDADVATPLHYAAYWGHEECVRILLEHNAPINVLNNDGYAPLHL 188
Cdd:pfam13857   2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 151-177 2.82e-06

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: 44.12  E-value: 2.82e-06
                           10        20
                   ....*....|....*....|....*..
gi 7296936     151 TPLHYAAYWGHEECVRILLEHNAPINV 177
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 214-363 3.29e-06

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 50.01  E-value: 3.29e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936  214 GKTALHMAIESKCAESARLLLQ---TNININDTDD--DGETPLMAAIACSMLDVAEELVKRGAriniqDKQNHTA----- 283
Cdd:cd22192  51 GETALHVAALYDNLEAAVVLMEaapELVNEPMTSDlyQGETALHIAVVNQNLNLVRELIARGA-----DVVSPRAtgtff 125

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936  284 --------------LQYAVRGRHTQMAKLLLERGARRLASQHL----LH-LAVESN---VKELVELLLQY---GESLSVW 338
Cdd:cd22192 126 rpgpknliyygehpLSFAACVGNEEIVRLLIEHGADIRAQDSLgntvLHiLVLQPNktfACQMYDLILSYdkeDDLQPLD 205

                       170       180
                ....*....|....*....|....*...
gi 7296936  339 NLKN---FTPIMLAIHRGRHEMLEYLLN 363
Cdd:cd22192 206 LVPNnqgLTPFKLAAKEGNIVMFQHLVQ 233
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 151-180 4.05e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 43.82  E-value: 4.05e-06
                          10        20        30
                  ....*....|....*....|....*....|.
gi 7296936    151 TPLHYAAY-WGHEECVRILLEHNAPINVLNN 180
Cdd:pfam00023   4 TPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
Ank_2 pfam12796
Ankyrin repeats (3 copies);
151-179 4.22e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 45.11  E-value: 4.22e-06
                          10        20
                  ....*....|....*....|....*....
gi 7296936    151 TPLHYAAYWGHEECVRILLEHNAPINVLN 179
Cdd:pfam12796  63 TALHYAARSGHLEIVKLLLEKGADINVKD 91
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 141-202 6.30e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.13  E-value: 6.30e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7296936   141 DPHLYDADVATPLHYAAYWGHEECVRILLEHNAPINVLNNDGYAPLHLGA--GFAGVTELLIKH 202
Cdd:PTZ00322 107 DPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEenGFREVVQLLSRH 170
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 214-363 4.45e-05

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: 46.68  E-value: 4.45e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936  214 GKTALHMAIESKCAESARLLLQTNININ-----------DTDDD---GETPLMAAIACSMLDVAEELVKRGAR-INIQDK 278
Cdd:cd22194 141 GQTALNIAIERRQGDIVKLLIAKGADVNahakgvffnpkYKHEGfyfGETPLALAACTNQPEIVQLLMEKESTdITSQDS 220

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936  279 QNHTALqyavrgrhtqmaklllergarrlasqHLLHLAVESN------VKELVELLLQY--GESL-SVWNLKNFTPIMLA 349
Cdd:cd22194 221 RGNTVL--------------------------HALVTVAEDSktqndfVKRMYDMILLKseNKNLeTIRNNEGLTPLQLA 274

                       170
                ....*....|....
gi 7296936  350 IHRGRHEMLEYLLN 363
Cdd:cd22194 275 AKMGKAEILKYILS 288
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 195-284 1.05e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 43.65  E-value: 1.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936   195 VTELLIKHGALVNAKTLSDGKTALHMAI---ESKCAESARLLLQTNININDTDDDGETPL-MAAIACSM-LDVAEELVKR 269
Cdd:PHA02859  68 ILKFLIENGADVNFKTRDNNLSALHHYLsfnKNVEPEILKILIDSGSSITEEDEDGKNLLhMYMCNFNVrINVIKLLIDS 147

                         90
                 ....*....|....*
gi 7296936   270 GARINIQDKQNHTAL 284
Cdd:PHA02859 148 GVSFLNKDFDNNNIL 162
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
260-455 1.12e-04

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 44.56  E-value: 1.12e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936  260 LDVAEELVKRGARINIQDKQNHTALQYAVRGRHTQMAKLLLERG----ARRLASQHLLHLAVESNVKELVELLLQYGESL 335
Cdd:COG0666   1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALlalaLADALGALLLLAAALAGDLLVALLLLAAGADI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936  336 SVWNLKNFTPIMLAIHRGRHEMLEYLLnvaeeqrKLGL---YSDVHDEGLVLFAVQQNFWvkefsRILRVLLAK--SPSA 410
Cdd:COG0666  81 NAKDDGGNTLLHAAARNGDLEIVKLLL-------EAGAdvnARDKDGETPLHLAAYNGNL-----EIVKLLLEAgaDVNA 148

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 7296936  411 RNDfydscaptivcgliYCHTPLSRAINLHRLEVAEFLIHEGCNL 455
Cdd:COG0666 149 QDN--------------DGNTPLHLAAANGNLEIVKLLLEAGADV 179
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 138-285 1.69e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 44.21  E-value: 1.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936   138 REHDPHLYDADVATPLHYAAYWGHEECVRILLEHNAPINVlnNDGYaplhlgagfaGVTELLIkhgalvnaktlsdgkta 217
Cdd:PHA02875 124 RGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDI--EDCC----------GCTPLII----------------- 174

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7296936   218 lhmAIESKCAESARLLLQTNININDTDDDGETPLMA-AIACSMLDVAEELVKRGARINIQ---DKQNHTALQ 285
Cdd:PHA02875 175 ---AMAKGDIAICKMLLDSGANIDYFGKNGCVAALCyAIENNKIDIVRLFIKRGADCNIMfmiEGEECTILD 243
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 165-247 3.43e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 43.73  E-value: 3.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936   165 VRILLEHNAPINVLNNDGYAPLHLGA--GFAGVTELLIKHGALVNAkTLSDGKTALHMAIESKCAESARLLLQTNININD 242
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACanGHVQVVRVLLEFGADPTL-LDKDGKTPLELAEENGFREVVQLLSRHSQCHFE 176


                 ....*
gi 7296936   243 TDDDG 247
Cdd:PTZ00322 177 LGANA 181
PHA02741 PHA02741
hypothetical protein; Provisional
 171-255 4.00e-04

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 41.57  E-value: 4.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936   171 HNAPINVLNNDGYAPLHLGAG------FAGVTELLIKHGALVNAKTLSDGKTALHMAIESKCAESARLLL-QTNININDT 243
Cdd:PHA02741  49 HAAALNATDDAGQMCIHIAAEkheaqlAAEIIDHLIELGADINAQEMLEGDTALHLAAHRRDHDLAEWLCcQPGIDLHFC 128

                         90
                 ....*....|..
gi 7296936   244 DDDGETPLMAAI 255
Cdd:PHA02741 129 NADNKSPFELAI 140
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 246-278 5.23e-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: 37.65  E-value: 5.23e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 7296936    246 DGETPLMAAIACSM-LDVAEELVKRGARINIQDK 278
Cdd:pfam00023   1 DGNTPLHLAAGRRGnLEIVKLLLSKGADVNARDK 34
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 151-177 7.37e-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: 37.24  E-value: 7.37e-04
                          10        20
                  ....*....|....*....|....*..
gi 7296936    151 TPLHYAAYWGHEECVRILLEHNAPINV 177
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 216-300 8.98e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.19  E-value: 8.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936   216 TALHMAIESKCAESA-------RLLLQTNININDTDDDGETPLMAAIACSMLDVAEELVKRGARINIQDKQNHTALQYAV 288
Cdd:PTZ00322  77 VVAHMLTVELCQLAAsgdavgaRILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAE 156

                         90
                 ....*....|..
gi 7296936   289 RGRHTQMAKLLL 300
Cdd:PTZ00322 157 ENGFREVVQLLS 168
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
 517-573 1.12e-03

SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more generic proteins that comprise a large family of E3 ubiquitin protein ligases.


Pssm-ID: 462192  Cd Length: 39  Bit Score: 36.76  E-value: 1.12e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 7296936    517 QPRSLQSLARLEIRRSLLRCLQtrpevqerylptqersslgRIVDEFAIPATLKRYL 573
Cdd:pfam07525   1 TPRSLQHLCRLAIRRALGKRRL-------------------GAIDKLPLPPLLKDYL 38
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 212-332 1.18e-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: 41.79  E-value: 1.18e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936  212 SDGKTALHMAIeskcaesarlllqtnININDTDDDGETPLMAAIACSmlDVAEELVKrgARINIQDKQNHTALQYAVRGR 291
Cdd:cd21882  24 ATGKTCLHKAA---------------LNLNDGVNEAIMLLLEAAPDS--GNPKELVN--APCTDEFYQGQTALHIAIENR 84

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 7296936  292 HTQMAKLLLERGARRLAS-----------------QHLLHLAVESNVKELVELLLQYG 332
Cdd:cd21882  85 NLNLVRLLVENGADVSARatgrffrkspgnlfyfgELPLSLAACTNQEEIVRLLLENG 142
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 213-242 1.73e-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: 36.03  E-value: 1.73e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 7296936     213 DGKTALHMAIESKCAESARLLLQTNININD 242
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
199-251 1.99e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.56  E-value: 1.99e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 7296936    199 LIKHG-ALVNAKTLsDGKTALHMAIESKCAESARLLLQTNININDTDDDGETPL 251
Cdd:pfam13857   1 LLEHGpIDLNRLDG-EGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 273-363 3.28e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 40.45  E-value: 3.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936    273 INIQDKQNHTALQY-AVRGRHTQMAKLLLERGARRLASQHLLHLAVEsNVKELVELLLQY-----GESLSVWNLKNF--- 343
Cdd:TIGR00870  45 INCPDRLGRSALFVaAIENENLELTELLLNLSCRGAVGDTLLHAISL-EYVDAVEAILLHllaafRKSGPLELANDQyts 123

                          90       100
                  ....*....|....*....|....*.
gi 7296936    344 ------TPIMLAIHRGRHEMLEYLLN 363
Cdd:TIGR00870 124 eftpgiTALHLAAHRQNYEIVKLLLE 149
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 146-228 3.78e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 40.43  E-value: 3.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936   146 DADVATPLHYAAYWGHE-ECVRILLEHNAPINVLNNDGYAPLHLGAGFAGVTELLIKHGA-----LVNAKTLSDGKTALH 219
Cdd:PHA02876 439 NKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAINIQNQYPLLIALEYHGIVNILLHYGAelrdsRVLHKSLNDNMFSFR 518


                 ....*....
gi 7296936   220 MAIESKCAE 228
Cdd:PHA02876 519 YIIAHICIQ 527
SOCS_ASB_like cd03716
SOCS (suppressors of cytokine signaling) box of ASB (ankyrin repeat and SOCS box) and SSB ...
 517-573 4.01e-03

SOCS (suppressors of cytokine signaling) box of ASB (ankyrin repeat and SOCS box) and SSB (SPRY domain-containing SOCS box proteins) protein families. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence of a variable number of repeats. SSB proteins contain a central SPRY domain and a C-terminal SOCS. Recently, it has been shown that all four SSB proteins interact with the MET, the receptor protein-tyrosine kinase for hepatocyte growth factor (HGF), and that SSB-1, SSB-2, and SSB-4 interact with prostate apoptosis response protein-4. Both types of interactions are mediated through the SPRY domain.


Pssm-ID: 239686  Cd Length: 42  Bit Score: 35.55  E-value: 4.01e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 7296936  517 QPRSLQSLARLEIRrsllRCLQTRPEVQerylptqersslgriVDEFAIPATLKRYL 573
Cdd:cd03716   2 TPRSLQHLCRLAIR----RCLGRRRLEL---------------IKKLPLPPRLKDYL 39
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 198-272 4.07e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 38.32  E-value: 4.07e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7296936   198 LLIKHGALVNAKTLSDGKTALHMAIESKCAESARLLL-QTNININDTDDDGETPLMAAIACSMLDVAEELVKRGAR 272
Cdd:PHA02736  76 LLMEWGADINGKERVFGNTPLHIAVYTQNYELATWLCnQPGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGAQ 151
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 213-245 4.60e-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: 4.60e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 7296936    213 DGKTALHMAIES-KCAESARLLLQTNININDTDD 245
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 254-362 4.81e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 39.59  E-value: 4.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7296936   254 AIACSMLDVAEELVKRGARINIQDKQNHTALQYAVRGRHTQMAKLLLERGA----RRLASQHLLHLAVESNVKELVELLL 329
Cdd:PHA02875   9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAipdvKYPDIESELHDAVEEGDVKAVEELL 88

                         90       100       110
                 ....*....|....*....|....*....|....
gi 7296936   330 QYGESLS-VWNLKNFTPIMLAIHRGRHEMLEYLL 362
Cdd:PHA02875  89 DLGKFADdVFYKDGMTPLHLATILKKLDIMKLLI 122
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 246-275 8.27e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.10  E-value: 8.27e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 7296936     246 DGETPLMAAIACSMLDVAEELVKRGARINI 275
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
SOCS cd03587
SOCS (suppressors of cytokine signaling) box. The SOCS box is found in the C-terminal region ...
 517-573 8.28e-03

SOCS (suppressors of cytokine signaling) box. The SOCS box is found in the C-terminal region of CIS/SOCS family proteins (in combination with a SH2 domain), ASBs (ankyrin repeat-containing proteins with a SOCS box), SSBs (SPRY domain-containing proteins with a SOCS box), and WSBs (WD40 repeat-containing proteins with a SOCS box), as well as, other miscellaneous proteins. The function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


Pssm-ID: 239641  Cd Length: 41  Bit Score: 34.37  E-value: 8.28e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 7296936  517 QPRSLQSLARLEIRrsllRCLQTRPEVQerylptqersslgriVDEFAIPATLKRYL 573
Cdd:cd03587   1 NPRSLQHLCRLAIR----RCLGKRRLDL---------------IDKLPLPPRLKDYL 38
 
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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