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Conserved domains on  [gi|442626107|ref|NP_001260081|]
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uncharacterized protein Dmel_CG9121, isoform C [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];
54-275 5.55e-44

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 157.04  E-value: 5.55e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107  54 DPHLYDADVATPLHYAAYWGHEECVRILLEHNAPINVLNNDGYAPLHLGA--GFAGVTELLIKHGALVNAKTlSDGKTAL 131
Cdd:COG0666   46 ALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAArnGDLEIVKLLLEAGADVNARD-KDGETPL 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107 132 HMAIESKCAESARLLLQTNININDTDDDGETPLMAAIACSMLDVAEELVKRGARINIQDKQNHTALQYAVRGRHTQMAKL 211
Cdd:COG0666  125 HLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKL 204

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442626107 212 LLERGARRLASQH----LLHLAVESNVKELVELLLQYGESLSVWNLKNFTPIMLAIHRGRHEMLEYLL 275
Cdd:COG0666  205 LLEAGADVNAKDNdgktALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLL 272
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
 430-486 1.31e-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: 36.37  E-value: 1.31e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 442626107  430 QPRSLQSLARLEIRRSLLRCLQtrpevqerylptqersslgRIVDEFAIPATLKRYL 486
Cdd:pfam07525   1 TPRSLQHLCRLAIRRALGKRRL-------------------GAIDKLPLPPLLKDYL 38
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
54-275 5.55e-44

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 157.04  E-value: 5.55e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107  54 DPHLYDADVATPLHYAAYWGHEECVRILLEHNAPINVLNNDGYAPLHLGA--GFAGVTELLIKHGALVNAKTlSDGKTAL 131
Cdd:COG0666   46 ALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAArnGDLEIVKLLLEAGADVNARD-KDGETPL 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107 132 HMAIESKCAESARLLLQTNININDTDDDGETPLMAAIACSMLDVAEELVKRGARINIQDKQNHTALQYAVRGRHTQMAKL 211
Cdd:COG0666  125 HLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKL 204

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442626107 212 LLERGARRLASQH----LLHLAVESNVKELVELLLQYGESLSVWNLKNFTPIMLAIHRGRHEMLEYLL 275
Cdd:COG0666  205 LLEAGADVNAKDNdgktALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLL 272
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 53-217 1.99e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 93.58  E-value: 1.99e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107  53 HDPHLYDADVATPLHYAAYWGHE-----ECVRILLEHNAPINVLNNDGYAPLHLGA----GFAGVTELLIKHGALVNAKT 123
Cdd:PHA03100  59 ADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAIskksNSYSIVEYLLDNGANVNIKN 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107 124 lSDGKTALHMAIESKCAES--ARLLLQTNININ----------------DTDDDGETPLMAAIACSMLDVAEELVKRGAR 185
Cdd:PHA03100 139 -SDGENLLHLYLESNKIDLkiLKLLIDKGVDINaknrvnyllsygvpinIKDVYGFTPLHYAVYNNNPEFVKYLLDLGAN 217

                        170       180       190
                 ....*....|....*....|....*....|..
gi 442626107 186 INIQDKQNHTALQYAVRGRHTQMAKLLLERGA 217
Cdd:PHA03100 218 PNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249
Ank_2 pfam12796
Ankyrin repeats (3 copies);
66-157 2.35e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.77  E-value: 2.35e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107   66 LHYAAYWGHEECVRILLEHNAPINVLNNDGYAPLHL--GAGFAGVTELLIKHgalVNAKTLSDGKTALHMAIESKCAESA 143
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLaaKNGHLEIVKLLLEH---ADVNLKDNGRTALHYAARSGHLEIV 77

                          90
                  ....*....|....
gi 442626107  144 RLLLQTNININDTD 157
Cdd:pfam12796  78 KLLLEKGADINVKD 91
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 108-283 3.24e-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: 53.16  E-value: 3.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107  108 VTELLIKHGALVnaktlSDGKTALHMAIESK---CAESARLLLQ------TNININDTDDD----GETPLMAAIACSMLD 174
Cdd:TIGR00870  68 LTELLLNLSCRG-----AVGDTLLHAISLEYvdaVEAILLHLLAafrksgPLELANDQYTSeftpGITALHLAAHRQNYE 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107  175 VAEELVKRGARINI-------QDKQNHTALQYavrGRH----------TQMAKLLLERGARRLA----SQHLLHLAVESN 233
Cdd:TIGR00870 143 IVKLLLERGASVPAracgdffVKSQGVDSFYH---GESplnaaaclgsPSIVALLSEDPADILTadslGNTLLHLLVMEN 219

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442626107  234 V-----KELV----ELLLQYGESLS-------VWNLKNFTPIMLAIHRGRHEMLEYLLNVAEEQRK 283
Cdd:TIGR00870 220 EfkaeyEELScqmyNFALSLLDKLRdskelevILNHQGLTPLKLAAKEGRIVLFRLKLAIKYKQKK 285
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 127-276 3.02e-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: 3.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107 127 GKTALHMAIESKCAESARLLLQ---TNININDTDD--DGETPLMAAIACSMLDVAEELVKRGAriniqDKQNHTA----- 196
Cdd:cd22192   51 GETALHVAALYDNLEAAVVLMEaapELVNEPMTSDlyQGETALHIAVVNQNLNLVRELIARGA-----DVVSPRAtgtff 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107 197 --------------LQYAVRGRHTQMAKLLLERGARRLASQHL----LH-LAVESN---VKELVELLLQY---GESLSVW 251
Cdd:cd22192  126 rpgpknliyygehpLSFAACVGNEEIVRLLIEHGADIRAQDSLgntvLHiLVLQPNktfACQMYDLILSYdkeDDLQPLD 205

                        170       180
                 ....*....|....*....|....*...
gi 442626107 252 NLKN---FTPIMLAIHRGRHEMLEYLLN 276
Cdd:cd22192  206 LVPNnqgLTPFKLAAKEGNIVMFQHLVQ 233
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 64-90 3.22e-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: 43.73  E-value: 3.22e-06
                           10        20
                   ....*....|....*....|....*..
gi 442626107    64 TPLHYAAYWGHEECVRILLEHNAPINV 90
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
 430-486 1.31e-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: 36.37  E-value: 1.31e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 442626107  430 QPRSLQSLARLEIRRSLLRCLQtrpevqerylptqersslgRIVDEFAIPATLKRYL 486
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 ...
 430-486 4.84e-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: 34.78  E-value: 4.84e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 442626107 430 QPRSLQSLARLEIRrsllRCLQTRPEVQerylptqersslgriVDEFAIPATLKRYL 486
Cdd:cd03716    2 TPRSLQHLCRLAIR----RCLGRRRLEL---------------IKKLPLPPRLKDYL 39
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
54-275 5.55e-44

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 157.04  E-value: 5.55e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107  54 DPHLYDADVATPLHYAAYWGHEECVRILLEHNAPINVLNNDGYAPLHLGA--GFAGVTELLIKHGALVNAKTlSDGKTAL 131
Cdd:COG0666   46 ALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAArnGDLEIVKLLLEAGADVNARD-KDGETPL 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107 132 HMAIESKCAESARLLLQTNININDTDDDGETPLMAAIACSMLDVAEELVKRGARINIQDKQNHTALQYAVRGRHTQMAKL 211
Cdd:COG0666  125 HLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKL 204

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442626107 212 LLERGARRLASQH----LLHLAVESNVKELVELLLQYGESLSVWNLKNFTPIMLAIHRGRHEMLEYLL 275
Cdd:COG0666  205 LLEAGADVNAKDNdgktALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLL 272
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
57-276 1.23e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 142.79  E-value: 1.23e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107  57 LYDADVATPLHYAAYWGHEECVRILLEHNAPINVLNNDGYAPLHL--GAGFAGVTELLIKHGALVNAKTlSDGKTALHMA 134
Cdd:COG0666   16 LLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAaaLAGDLLVALLLLAAGADINAKD-DGGNTLLHAA 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107 135 IESKCAESARLLLQTNININDTDDDGETPLMAAIACSMLDVAEELVKRGARINIQDKQNHTALQYAVRGRHTQMAKLLLE 214
Cdd:COG0666   95 ARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLE 174

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442626107 215 RGA----RRLASQHLLHLAVESNVKELVELLLQYGESLSVWNLKNFTPIMLAIHRGRHEMLEYLLN 276
Cdd:COG0666  175 AGAdvnaRDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
54-229 1.25e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 140.09  E-value: 1.25e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107  54 DPHLYDADVATPLHYAAYWGHEECVRILLEHNAPINVLNNDGYAPLHLGA--GFAGVTELLIKHGALVNAKTlSDGKTAL 131
Cdd:COG0666  112 DVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAanGNLEIVKLLLEAGADVNARD-NDGETPL 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107 132 HMAIESKCAESARLLLQTNININDTDDDGETPLMAAIACSMLDVAEELVKRGARINIQDKQNHTALQYAVRGRHTQMAKL 211
Cdd:COG0666  191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270

                        170
                 ....*....|....*...
gi 442626107 212 LLERGARRLASQHLLHLA 229
Cdd:COG0666  271 LLLALLLLAAALLDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
80-276 8.78e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 123.91  E-value: 8.78e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107  80 ILLEHNAPINVLNNDGYAPLHLGAGFAGVTELLIKHGALVNAKTLSDGKTALHMAIESKCAESARLLLQTNININDTDDD 159
Cdd:COG0666    7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107 160 GETPLMAAIACSMLDVAEELVKRGARINIQDKQNHTALQYAVRGRHTQMAKLLLERGA----RRLASQHLLHLAVESNVK 235
Cdd:COG0666   87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGAdvnaQDNDGNTPLHLAAANGNL 166

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 442626107 236 ELVELLLQYGESLSVWNLKNFTPIMLAIHRGRHEMLEYLLN 276
Cdd:COG0666  167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLE 207
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
54-197 1.36e-27

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 111.97  E-value: 1.36e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107  54 DPHLYDADVATPLHYAAYWGHEECVRILLEHNAPINVLNNDGYAPLHLGA--GFAGVTELLIKHGALVNAKTlSDGKTAL 131
Cdd:COG0666  145 DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAenGHLEIVKLLLEAGADVNAKD-NDGKTAL 223

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442626107 132 HMAIESKCAESARLLLQTNININDTDDDGETPLMAAIACSMLDVAEELVKRGARINIQDKQNHTAL 197
Cdd:COG0666  224 DLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
111-276 1.62e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 91.94  E-value: 1.62e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107 111 LLIKHGALVNAKTLSDGKTALHMAIESKCAESARLLLQTNININDTDDDGETPLMAAIACSMLDVAEELVKRGARINIQD 190
Cdd:COG0666    5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107 191 KQNHTALQYAVRGRHTQMAKLLLERGA----RRLASQHLLHLAVESNVKELVELLLQYGESLSVWNLKNFTPIMLAIHRG 266
Cdd:COG0666   85 DGGNTLLHAAARNGDLEIVKLLLEAGAdvnaRDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANG 164

                        170
                 ....*....|
gi 442626107 267 RHEMLEYLLN 276
Cdd:COG0666  165 NLEIVKLLLE 174
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 53-217 1.99e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 93.58  E-value: 1.99e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107  53 HDPHLYDADVATPLHYAAYWGHE-----ECVRILLEHNAPINVLNNDGYAPLHLGA----GFAGVTELLIKHGALVNAKT 123
Cdd:PHA03100  59 ADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAIskksNSYSIVEYLLDNGANVNIKN 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107 124 lSDGKTALHMAIESKCAES--ARLLLQTNININ----------------DTDDDGETPLMAAIACSMLDVAEELVKRGAR 185
Cdd:PHA03100 139 -SDGENLLHLYLESNKIDLkiLKLLIDKGVDINaknrvnyllsygvpinIKDVYGFTPLHYAVYNNNPEFVKYLLDLGAN 217

                        170       180       190
                 ....*....|....*....|....*....|..
gi 442626107 186 INIQDKQNHTALQYAVRGRHTQMAKLLLERGA 217
Cdd:PHA03100 218 PNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 66-276 6.92e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 92.04  E-value: 6.92e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107  66 LHYAAYWGHEECVRILLEHNAPINVLNNDG-----YAPLHLG--AGFAGVTELLIKHGALVNAKTLSDgKTALH-----M 133
Cdd:PHA03100   1 LYSYIVLTKSRIIKVKNIKYIIMEDDLNDYsykkpVLPLYLAkeARNIDVVKILLDNGADINSSTKNN-STPLHylsniK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107 134 AIESKCAESARLLLQTNININDTDDDGETPLMAAIACSM--LDVAEELVKRGARINIQDKQNHTALQYAVRGRH--TQMA 209
Cdd:PHA03100  80 YNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKKSnsYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKIL 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442626107 210 KLLLERGarrlasqhllhlaVESNVKELVELLLQYGESLSVWNLKNFTPIMLAIHRGRHEMLEYLLN 276
Cdd:PHA03100 160 KLLIDKG-------------VDINAKNRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLD 213
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 106-263 2.07e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 88.01  E-value: 2.07e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107 106 AGVTELLIKHGALVNAKTLSDGKTALHMAIESKCAESARLLLQTNININDTDDDGETPLMAAIACSMLDVAEELVKRGAR 185
Cdd:PHA02878 147 AEITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS 226

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107 186 INIQDKQNHTALQYAV-RGRHTQMAKLLLERGARRLASQHL-----LHLAVESNVKelVELLLQYGESLSVWNLKNFTPI 259
Cdd:PHA02878 227 TDARDKCGNTPLHISVgYCKDYDILKLLLEHGVDVNAKSYIlgltaLHSSIKSERK--LKLLLEYGADINSLNSYKLTPL 304


                 ....
gi 442626107 260 MLAI 263
Cdd:PHA02878 305 SSAV 308
Ank_2 pfam12796
Ankyrin repeats (3 copies);
66-157 2.35e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.77  E-value: 2.35e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107   66 LHYAAYWGHEECVRILLEHNAPINVLNNDGYAPLHL--GAGFAGVTELLIKHgalVNAKTLSDGKTALHMAIESKCAESA 143
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLaaKNGHLEIVKLLLEH---ADVNLKDNGRTALHYAARSGHLEIV 77

                          90
                  ....*....|....
gi 442626107  144 RLLLQTNININDTD 157
Cdd:pfam12796  78 KLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
131-217 1.77e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.77  E-value: 1.77e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107  131 LHMAIESKCAESARLLLQTNININDTDDDGETPLMAAIACSMLDVAEELVKRgARINIQDkQNHTALQYAVRGRHTQMAK 210
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78


                  ....*..
gi 442626107  211 LLLERGA 217
Cdd:pfam12796  79 LLLEKGA 85
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 64-192 4.37e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 80.48  E-value: 4.37e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107  64 TPLHYAAYW--GHEECVRILLEHNAPINVLNNDGYAPLHLGAGFAGVT----ELLIKHGALVNAKTLSD----------- 126
Cdd:PHA03100 108 TPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkilKLLIDKGVDINAKNRVNyllsygvpini 187

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107 127 ----GKTALHMAIESKCAESARLLLQTNININDTDDDGETPLMAAIACSMLDVAEELVKRGARINIQDKQ 192
Cdd:PHA03100 188 kdvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
PHA03095 PHA03095
ankyrin-like protein; Provisional
 58-276 3.52e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 77.76  E-value: 3.52e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107  58 YDADVA-------TPLHYAAYWGHEEC---VRILLEHNAPINVLNNDGYAPLHLGAGFA---GVTELLIKHGALVNAKTL 124
Cdd:PHA03095  36 AGADVNfrgeygkTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLHLYLYNAttlDVIKLLIKAGADVNAKDK 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107 125 SdGKTALHMAIESKC--AESARLLLQTNININDTDDDGETP-----------------LMAAIAC---------SMLD-- 174
Cdd:PHA03095 116 V-GRTPLHVYLSGFNinPKVIRLLLRKGADVNALDLYGMTPlavllksrnanvellrlLIDAGADvyavddrfrSLLHhh 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107 175 ---------VAEELVKRGARINIQDKQNHTALQYAVRG---RHTQMAKLLlERG----ARRLASQHLLHLAVESNVKELV 238
Cdd:PHA03095 195 lqsfkprarIVRELIRAGCDPAATDMLGNTPLHSMATGsscKRSLVLPLL-IAGisinARNRYGQTPLHYAAVFNNPRAC 273

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 442626107 239 ELLLQYGESLSVWNLKNFTPIMLAIHRGRHEMLEYLLN 276
Cdd:PHA03095 274 RRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALA 311
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 54-276 6.18e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 76.57  E-value: 6.18e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107  54 DPHLYDADVATPLHYAAYWGHEECVRILLEHNAPINVLNNDGYAPLH--LGAGFAGVTELLIKHGALVNAKTLSDGKTAL 131
Cdd:PHA02875  27 NPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHdaVEEGDVKAVEELLDLGKFADDVFYKDGMTPL 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107 132 HMAIESKCAESARLLLQTNININDTDDDGETPLMAAIACSMLDVAEELVKRGARINIQDKQNHTALQYAVRGRHTQMAKL 211
Cdd:PHA02875 107 HLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKM 186

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107 212 LLERGAR-----RLASQHLLHLAVESNVKELVELLLQYGESLSvwnlknftpIMLAIHRGRHEMLEYLLN 276
Cdd:PHA02875 187 LLDSGANidyfgKNGCVAALCYAIENNKIDIVRLFIKRGADCN---------IMFMIEGEECTILDMICN 247
Ank_2 pfam12796
Ankyrin repeats (3 copies);
164-250 1.13e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 69.37  E-value: 1.13e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107  164 LMAAIACSMLDVAEELVKRGARINIQDKQNHTALQYAVRGRHTQMAKLLLERGARRLASQHL--LHLAVESNVKELVELL 241
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRtaLHYAARSGHLEIVKLL 80


                  ....*....
gi 442626107  242 LQYGESLSV 250
Cdd:pfam12796  81 LEKGADINV 89
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 57-282 3.88e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 75.10  E-value: 3.88e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107  57 LYDADVA---------TPLHYAAYWGH-EECVRILLEHNAPINVLNNDGYAPLHLGAGFAGVTE---LLIKHGALVNAkT 123
Cdd:PHA02876 259 LYDAGFSvnsiddcknTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYDTEnirTLIMLGADVNA-A 337

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107 124 LSDGKTALHMAIE-SKCAESARLLLQTNININDTDDDGETPLMAAIACSMLDVAEELVKRGARINIQDKQNHTALQYAVR 202
Cdd:PHA02876 338 DRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALC 417

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107 203 GRHTQMA-KLLLERGAR-RLASQHL---LHLAVESNVK-ELVELLLQYGESLSVWNLKNFTPIMLAIhrGRHEMLEYLLN 276
Cdd:PHA02876 418 GTNPYMSvKTLIDRGANvNSKNKDLstpLHYACKKNCKlDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLH 495


                 ....*.
gi 442626107 277 VAEEQR 282
Cdd:PHA02876 496 YGAELR 501
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 64-168 6.86e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 70.68  E-value: 6.86e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107  64 TPLHYAAYWGHEECVRILLEHNAPINVLNNDGYAPLHLGAGFA---GVTELLIKHGALVNAKTLSDGKTALHMAIESKca 140
Cdd:PHA02878 203 SPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCkdyDILKLLLEHGVDVNAKSYILGLTALHSSIKSE-- 280

                         90       100
                 ....*....|....*....|....*...
gi 442626107 141 ESARLLLQTNININDTDDDGETPLMAAI 168
Cdd:PHA02878 281 RKLKLLLEYGADINSLNSYKLTPLSSAV 308
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 54-202 1.67e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 69.22  E-value: 1.67e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107  54 DPHLYDADVATPLHYAAYWGHEECVRILLEHNAPINVLNNDGYAPLHLG--AGFAGVTELLIKHGALVNAKTlSDGKTAL 131
Cdd:PHA02874 116 DVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAikHNFFDIIKLLLEKGAYANVKD-NNGESPL 194

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442626107 132 HMAIESKCAESARLLLQTNININDTDDDGETPLMAAIACSMLDVaeELVKRGARINIQDKQNHTALQYAVR 202
Cdd:PHA02874 195 HNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAI--ELLINNASINDQDIDGSTPLHHAIN 263
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 64-284 2.09e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 69.71  E-value: 2.09e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107  64 TPLHYAAYWGHEECVRILLEHNAPINVLNNDGYAPLHLGAGFAGVTEL--LIKHGALVNAKTLSdgktaLHMAIESKCAE 141
Cdd:PHA02876 180 TPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIkaIIDNRSNINKNDLS-----LLKAIRNEDLE 254

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107 142 SARLLLQTNININDTDDDGETPLMAAI-ACSMLDVAEELVKRGARINIQDKQNHTALQ-YAVRGRHTQMAKLLLERGARR 219
Cdd:PHA02876 255 TSLLLYDAGFSVNSIDDCKNTPLHHASqAPSLSRLVPKLLERGADVNAKNIKGETPLYlMAKNGYDTENIRTLIMLGADV 334

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107 220 LASQHL----LHLAVE-SNVKELVELLLQYGESLSVWNLKNFTPIMLAIHRGRHEMLEYLLNVAEEQRKL 284
Cdd:PHA02876 335 NAADRLyitpLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEAL 404
PHA03095 PHA03095
ankyrin-like protein; Provisional
 64-215 5.00e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 64.66  E-value: 5.00e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107  64 TPLH-YAA-YWGHEECVRILLEHNAPINVLNNDGYAPLHLGAGFAGVT----ELLIKHGA----------------LVNA 121
Cdd:PHA03095 119 TPLHvYLSgFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANvellRLLIDAGAdvyavddrfrsllhhhLQSF 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107 122 K------------------TLSDGKTALH-MAIESKCAESARL-LLQTNININDTDDDGETPLMAAiACSMLDVA-EELV 180
Cdd:PHA03095 199 KprarivreliragcdpaaTDMLGNTPLHsMATGSSCKRSLVLpLLIAGISINARNRYGQTPLHYA-AVFNNPRAcRRLI 277

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 442626107 181 KRGARINIQDKQNHTALQYAVRGRHTQMAKLLLER 215
Cdd:PHA03095 278 ALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAK 312
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 59-191 9.15e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 63.83  E-value: 9.15e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107  59 DADVATPLHYAAYWGHEECVRILLEHNAPINVLNNDGYAPLHLGAGF-AGVTELLIKHgALVNAKTLsDGKTALHMAIES 137
Cdd:PHA02874 187 DNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHnRSAIELLINN-ASINDQDI-DGSTPLHHAINP 264

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 442626107 138 KCA-ESARLLLQTNININDTDDDGETPLMAAIA-CSMLDVAEELVKRGARINIQDK 191
Cdd:PHA02874 265 PCDiDIIDILLYHKADISIKDNKGENPIDTAFKyINKDPVIKDIIANAVLIKEADK 320
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 61-264 1.04e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 63.83  E-value: 1.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107  61 DVATPLHYAAYWGHEECVRILLEHNAPINVLNNDGYAPL--HLGAGFAGVTELLIKHGA--------------------- 117
Cdd:PHA02874  34 ETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLltAIKIGAHDIIKLLIDNGVdtsilpipciekdmiktildc 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107 118 --LVNAKTlSDGKTALHMAIESKCAESARLLLQTNININDTDDDGETPLMAAIACSMLDVAEELVKRGARINIQDKQNHT 195
Cdd:PHA02874 114 giDVNIKD-AELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGES 192

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442626107 196 ALQYAVRGRHTQMAKLLLERGARRLASQHL----LHLAVESNvKELVELLLQyGESLSVWNLKNFTPIMLAIH 264
Cdd:PHA02874 193 PLHNAAEYGDYACIKLLIDHGNHIMNKCKNgftpLHNAIIHN-RSAIELLIN-NASINDQDIDGSTPLHHAIN 263
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 103-276 1.18e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 63.44  E-value: 1.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107 103 AGFAGVTELLIKHGALVNAKTlSDGKTALHMAIESKCAESARLLLqtninindtdDDGETPLMAAIACSMLDVAEELVKR 182
Cdd:PHA02874  45 SGDAKIVELFIKHGADINHIN-TKIPHPLLTAIKIGAHDIIKLLI----------DNGVDTSILPIPCIEKDMIKTILDC 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107 183 GARINIQDKQNHTALQYAVRGRHTQMAKLLLERGA----RRLASQHLLHLAVESNVKELVELLLQYGESLSVWNLKNFTP 258
Cdd:PHA02874 114 GIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGAdvniEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESP 193

                        170
                 ....*....|....*...
gi 442626107 259 IMLAIHRGRHEMLEYLLN 276
Cdd:PHA02874 194 LHNAAEYGDYACIKLLID 211
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 54-217 1.47e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 63.73  E-value: 1.47e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107  54 DPHLYDADVATPLHYAAYWGHEECVRILLEHNAPINVLNndgyaplhlgagfagvtellikhgalvnaktlSDGKTALHM 133
Cdd:PLN03192 550 DPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRD--------------------------------ANGNTALWN 597

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107 134 AIESKCAESARLLLQTNiNINDTDDDGETPLMAAIAcSMLDVAEELVKRGARINIQDKQNHTALQYAVRGRHTQMAKLLL 213
Cdd:PLN03192 598 AISAKHHKIFRILYHFA-SISDPHAAGDLLCTAAKR-NDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLI 675


                 ....
gi 442626107 214 ERGA 217
Cdd:PLN03192 676 MNGA 679
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 65-293 5.28e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 58.35  E-value: 5.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107  65 PLHYAAYWGHEECVRILLEHNAPINVLNNDGYAPLHL---GAGFAGVTELLikhgALVNAKTLSDGKTALHMAIESKCAE 141
Cdd:PHA02878  40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIickEPNKLGMKEMI----RSINKCSVFYTLVAIKDAFNNRNVE 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107 142 SARLLLQTNININDTDDDGETPLMAAIACSMLDVAEELVKRGARINIQDK-QNHTALQYAVRGRHTQMAKLLLERGAR-- 218
Cdd:PHA02878 116 IFKIILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANvn 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107 219 --RLASQHLLHLAVESNVKELVELLLQYGESLSVWNLKNFTPIMLAIHRGR-HEMLEYLL------NVAEEQRKL-GLYS 288
Cdd:PHA02878 196 ipDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKdYDILKLLLehgvdvNAKSYILGLtALHS 275


                 ....*
gi 442626107 289 DVHDE 293
Cdd:PHA02878 276 SIKSE 280
PHA03095 PHA03095
ankyrin-like protein; Provisional
 54-154 1.08e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 57.34  E-value: 1.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107  54 DPHLYDADVATPLHYAAYwgHEECVRI----LLEHNAPINVLNNDGYAPLHLGAGF--AGVTELLIKHGALVNAKTlSDG 127
Cdd:PHA03095 214 DPAATDMLGNTPLHSMAT--GSSCKRSlvlpLLIAGISINARNRYGQTPLHYAAVFnnPRACRRLIALGADINAVS-SDG 290

                         90       100
                 ....*....|....*....|....*..
gi 442626107 128 KTALHMAIESKCAESARLLLQTNININ 154
Cdd:PHA03095 291 NTPLSLMVRNNNGRAVRAALAKNPSAE 317
Ank_2 pfam12796
Ankyrin repeats (3 copies);
226-278 1.85e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 51.66  E-value: 1.85e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 442626107  226 LHLAVESNVKELVELLLQYGESLSVWNLKNFTPIMLAIHRGRHEMLEYLLNVA 278
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA 53
Ank_4 pfam13637
Ankyrin repeats (many copies);
64-113 2.54e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.35  E-value: 2.54e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 442626107   64 TPLHYAAYWGHEECVRILLEHNAPINVLNNDGYAPLHLGA--GFAGVTELLI 113
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAAsnGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
145-200 8.90e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.88  E-value: 8.90e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 442626107  145 LLLQTNININDTDDDGETPLMAAIACSMLDVAEELVKRGARINIQDKQNHTALQYA 200
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 131-292 2.09e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.43  E-value: 2.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107 131 LHMAIESKCAESARLLLQTNIN-INDTDDDGETPLMAAIACSMLDVAEELVKRGARINIQDKQNHTALQYAVRGRHTQMA 209
Cdd:PHA02874   5 LRMCIYSGDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDII 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107 210 KLLLERGA---------------------------RRLASQHLLHLAVESNVKELVELLLQYGESLSVWNLKNFTPIMLA 262
Cdd:PHA02874  85 KLLIDNGVdtsilpipciekdmiktildcgidvniKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIA 164

                        170       180       190
                 ....*....|....*....|....*....|
gi 442626107 263 IHRGRHEMLEYLLnvaeeqrKLGLYSDVHD 292
Cdd:PHA02874 165 IKHNFFDIIKLLL-------EKGAYANVKD 187
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 108-283 3.24e-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: 53.16  E-value: 3.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107  108 VTELLIKHGALVnaktlSDGKTALHMAIESK---CAESARLLLQ------TNININDTDDD----GETPLMAAIACSMLD 174
Cdd:TIGR00870  68 LTELLLNLSCRG-----AVGDTLLHAISLEYvdaVEAILLHLLAafrksgPLELANDQYTSeftpGITALHLAAHRQNYE 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107  175 VAEELVKRGARINI-------QDKQNHTALQYavrGRH----------TQMAKLLLERGARRLA----SQHLLHLAVESN 233
Cdd:TIGR00870 143 IVKLLLERGASVPAracgdffVKSQGVDSFYH---GESplnaaaclgsPSIVALLSEDPADILTadslGNTLLHLLVMEN 219

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442626107  234 V-----KELV----ELLLQYGESLS-------VWNLKNFTPIMLAIHRGRHEMLEYLLNVAEEQRK 283
Cdd:TIGR00870 220 EfkaeyEELScqmyNFALSLLDKLRdskelevILNHQGLTPLKLAAKEGRIVLFRLKLAIKYKQKK 285
PHA03095 PHA03095
ankyrin-like protein; Provisional
 139-398 4.40e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 52.33  E-value: 4.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107 139 CAESARLLLQTNININDTDDDGETPLMAAIACSMLDVAEE---LVKRGARINIQDKQNHTALQYAVRGRHT-QMAKLLLE 214
Cdd:PHA03095  26 TVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIK 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107 215 RGARRLAS----QHLLH--LAVESNVKELVELLLQYGESLSVWNLKNFTP--IMLAIHRGRHEMLEYLLNVAEEQRklgl 286
Cdd:PHA03095 106 AGADVNAKdkvgRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPlaVLLKSRNANVELLRLLIDAGADVY---- 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107 287 ysDVHDEGLVLFAVQQNFwVKEFSRILRVLLAK--SPSARNDF----------YDSCAPTIVCGLI-----------YCH 343
Cdd:PHA03095 182 --AVDDRFRSLLHHHLQS-FKPRARIVRELIRAgcDPAATDMLgntplhsmatGSSCKRSLVLPLLiagisinarnrYGQ 258

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 442626107 344 TPLSRAINLHRLEVAEFLIHEGCNLAqicrehvvneLRSNCTPTRLAFARLLCNA 398
Cdd:PHA03095 259 TPLHYAAVFNNPRACRRLIALGADIN----------AVSSDGNTPLSLMVRNNNG 303
PHA02798 PHA02798
ankyrin-like protein; Provisional
 59-276 5.13e-07

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 52.14  E-value: 5.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107  59 DADVATPL-----HYAAYWGHEECVRILLEHNAPINVLNNDGYAPLH--LGAGFAGVTELL---IKHGALVNAKTlSDGK 128
Cdd:PHA02798  68 DNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYclLSNGYINNLEILlfmIENGADTTLLD-KDGF 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107 129 TALHMAIESKCA---ESARLLLQTNININD-TDDDGETPL----MAAIACSMLDVAEELVKRGARINIQDKQNHtalqya 200
Cdd:PHA02798 147 TMLQVYLQSNHHidiEIIKLLLEKGVDINThNNKEKYDTLhcyfKYNIDRIDADILKLFVDNGFIINKENKSHK------ 220

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442626107 201 vrgrhtqmaKLLLErgarRLASQHLLHLAVESNVkelVELLLQYGEsLSVWNLKNFTPIMLAIHRGRHEMLEYLLN 276
Cdd:PHA02798 221 ---------KKFME----YLNSLLYDNKRFKKNI---LDFIFSYID-INQVDELGFNPLYYSVSHNNRKIFEYLLQ 279
Ank_4 pfam13637
Ankyrin repeats (many copies);
224-275 6.84e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.11  E-value: 6.84e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 442626107  224 HLLHLAVESNVKELVELLLQYGESLSVWNLKNFTPIMLAIHRGRHEMLEYLL 275
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
129-180 8.66e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.73  E-value: 8.66e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 442626107  129 TALHMAIESKCAESARLLLQTNININDTDDDGETPLMAAIACSMLDVAEELV 180
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
162-213 1.56e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.34  E-value: 1.56e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 442626107  162 TPLMAAIACSMLDVAEELVKRGARINIQDKQNHTALQYAVRGRHTQMAKLLL 213
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02798 PHA02798
ankyrin-like protein; Provisional
 108-216 1.56e-06

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 50.60  E-value: 1.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107 108 VTELLIKHGALVNAK----------TLSDGKTALHMaieskcAESARLLLQTNININDTDDDGETPLMAAIACSMLDVAE 177
Cdd:PHA02798  53 IVKLFINLGANVNGLdneystplctILSNIKDYKHM------LDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLE 126

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 442626107 178 EL---VKRGARINIQDKQNHTALQYAVRGRHT---QMAKLLLERG 216
Cdd:PHA02798 127 ILlfmIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKG 171
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 108-266 1.79e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 50.83  E-value: 1.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107 108 VTELLIKHGALVNAKTLSdGKTALHMAIESKCAESARLLLQTNININDTDDDGETPLMAAIACSMLDVAEELVKRGARIN 187
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIY-CITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNIN 238

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107 188 iqdkQNHTALQYAVRGRHTQMAKLLLERG----ARRLASQHLLHLAVES-NVKELVELLLQYGESLSVWNLKNFTPIMLA 262
Cdd:PHA02876 239 ----KNDLSLLKAIRNEDLETSLLLYDAGfsvnSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIKGETPLYLM 314


                 ....
gi 442626107 263 IHRG 266
Cdd:PHA02876 315 AKNG 318
Ank_5 pfam13857
Ankyrin repeats (many copies);
48-101 2.62e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.64  E-value: 2.62e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 442626107   48 VSCREHDPHLYDADVATPLHYAAYWGHEECVRILLEHNAPINVLNNDGYAPLHL 101
Cdd:pfam13857   2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 127-276 3.02e-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: 3.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107 127 GKTALHMAIESKCAESARLLLQ---TNININDTDD--DGETPLMAAIACSMLDVAEELVKRGAriniqDKQNHTA----- 196
Cdd:cd22192   51 GETALHVAALYDNLEAAVVLMEaapELVNEPMTSDlyQGETALHIAVVNQNLNLVRELIARGA-----DVVSPRAtgtff 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107 197 --------------LQYAVRGRHTQMAKLLLERGARRLASQHL----LH-LAVESN---VKELVELLLQY---GESLSVW 251
Cdd:cd22192  126 rpgpknliyygehpLSFAACVGNEEIVRLLIEHGADIRAQDSLgntvLHiLVLQPNktfACQMYDLILSYdkeDDLQPLD 205

                        170       180
                 ....*....|....*....|....*...
gi 442626107 252 NLKN---FTPIMLAIHRGRHEMLEYLLN 276
Cdd:cd22192  206 LVPNnqgLTPFKLAAKEGNIVMFQHLVQ 233
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 64-90 3.22e-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: 43.73  E-value: 3.22e-06
                           10        20
                   ....*....|....*....|....*..
gi 442626107    64 TPLHYAAYWGHEECVRILLEHNAPINV 90
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_2 pfam12796
Ankyrin repeats (3 copies);
64-92 3.93e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 45.11  E-value: 3.93e-06
                          10        20
                  ....*....|....*....|....*....
gi 442626107   64 TPLHYAAYWGHEECVRILLEHNAPINVLN 92
Cdd:pfam12796  63 TALHYAARSGHLEIVKLLLEKGADINVKD 91
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 64-93 4.23e-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: 43.43  E-value: 4.23e-06
                          10        20        30
                  ....*....|....*....|....*....|.
gi 442626107   64 TPLHYAAY-WGHEECVRILLEHNAPINVLNN 93
Cdd:pfam00023   4 TPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 54-115 4.76e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.13  E-value: 4.76e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442626107  54 DPHLYDADVATPLHYAAYWGHEECVRILLEHNAPINVLNNDGYAPLHLGA--GFAGVTELLIKH 115
Cdd:PTZ00322 107 DPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEenGFREVVQLLSRH 170
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 127-276 3.63e-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: 46.29  E-value: 3.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107 127 GKTALHMAIESKCAESARLLLQTNININ-----------DTDDD---GETPLMAAIACSMLDVAEELVKRGAR-INIQDK 191
Cdd:cd22194  141 GQTALNIAIERRQGDIVKLLIAKGADVNahakgvffnpkYKHEGfyfGETPLALAACTNQPEIVQLLMEKESTdITSQDS 220

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107 192 QNHTALqyavrgrhtqmaklllergarrlasqHLLHLAVESN------VKELVELLLQY--GESL-SVWNLKNFTPIMLA 262
Cdd:cd22194  221 RGNTVL--------------------------HALVTVAEDSktqndfVKRMYDMILLKseNKNLeTIRNNEGLTPLQLA 274

                        170
                 ....*....|....
gi 442626107 263 IHRGRHEMLEYLLN 276
Cdd:cd22194  275 AKMGKAEILKYILS 288
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 108-197 8.63e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 43.65  E-value: 8.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107 108 VTELLIKHGALVNAKTLSDGKTALHMAI---ESKCAESARLLLQTNININDTDDDGETPL-MAAIACSM-LDVAEELVKR 182
Cdd:PHA02859  68 ILKFLIENGADVNFKTRDNNLSALHHYLsfnKNVEPEILKILIDSGSSITEEDEDGKNLLhMYMCNFNVrINVIKLLIDS 147

                         90
                 ....*....|....*
gi 442626107 183 GARINIQDKQNHTAL 197
Cdd:PHA02859 148 GVSFLNKDFDNNNIL 162
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
173-368 1.26e-04

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 44.17  E-value: 1.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107 173 LDVAEELVKRGARINIQDKQNHTALQYAVRGRHTQMAKLLLERG----ARRLASQHLLHLAVESNVKELVELLLQYGESL 248
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALlalaLADALGALLLLAAALAGDLLVALLLLAAGADI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107 249 SVWNLKNFTPIMLAIHRGRHEMLEYLLnvaeeqrKLGL---YSDVHDEGLVLFAVQQNFWvkefsRILRVLLAK--SPSA 323
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLL-------EAGAdvnARDKDGETPLHLAAYNGNL-----EIVKLLLEAgaDVNA 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 442626107 324 RNDfydscaptivcgliYCHTPLSRAINLHRLEVAEFLIHEGCNL 368
Cdd:COG0666  149 QDN--------------DGNTPLHLAAANGNLEIVKLLLEAGADV 179
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 51-198 1.36e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 44.21  E-value: 1.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107  51 REHDPHLYDADVATPLHYAAYWGHEECVRILLEHNAPINVlnNDGYaplhlgagfaGVTELLIkhgalvnaktlsdgkta 130
Cdd:PHA02875 124 RGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDI--EDCC----------GCTPLII----------------- 174

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442626107 131 lhmAIESKCAESARLLLQTNININDTDDDGETPLMA-AIACSMLDVAEELVKRGARINIQ---DKQNHTALQ 198
Cdd:PHA02875 175 ---AMAKGDIAICKMLLDSGANIDYFGKNGCVAALCyAIENNKIDIVRLFIKRGADCNIMfmiEGEECTILD 243
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 78-160 2.42e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 43.73  E-value: 2.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107  78 VRILLEHNAPINVLNNDGYAPLHLGA--GFAGVTELLIKHGALVNAkTLSDGKTALHMAIESKCAESARLLLQTNININD 155
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACanGHVQVVRVLLEFGADPTL-LDKDGKTPLELAEENGFREVVQLLSRHSQCHFE 176


                 ....*
gi 442626107 156 TDDDG 160
Cdd:PTZ00322 177 LGANA 181
PHA02741 PHA02741
hypothetical protein; Provisional
 84-168 3.61e-04

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 41.57  E-value: 3.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107  84 HNAPINVLNNDGYAPLHLGAG------FAGVTELLIKHGALVNAKTLSDGKTALHMAIESKCAESARLLL-QTNININDT 156
Cdd:PHA02741  49 HAAALNATDDAGQMCIHIAAEkheaqlAAEIIDHLIELGADINAQEMLEGDTALHLAAHRRDHDLAEWLCcQPGIDLHFC 128

                         90
                 ....*....|..
gi 442626107 157 DDDGETPLMAAI 168
Cdd:PHA02741 129 NADNKSPFELAI 140
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 159-191 5.30e-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: 5.30e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 442626107  159 DGETPLMAAIACSM-LDVAEELVKRGARINIQDK 191
Cdd:pfam00023   1 DGNTPLHLAAGRRGnLEIVKLLLSKGADVNARDK 34
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 129-213 6.68e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.19  E-value: 6.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107 129 TALHMAIESKCAESA-------RLLLQTNININDTDDDGETPLMAAIACSMLDVAEELVKRGARINIQDKQNHTALQYAV 201
Cdd:PTZ00322  77 VVAHMLTVELCQLAAsgdavgaRILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAE 156

                         90
                 ....*....|..
gi 442626107 202 RGRHTQMAKLLL 213
Cdd:PTZ00322 157 ENGFREVVQLLS 168
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 64-90 8.24e-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: 8.24e-04
                          10        20
                  ....*....|....*....|....*..
gi 442626107   64 TPLHYAAYWGHEECVRILLEHNAPINV 90
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADINA 30
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 125-245 9.83e-04

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 41.79  E-value: 9.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107 125 SDGKTALHMAIeskcaesarlllqtnININDTDDDGETPLMAAIACSmlDVAEELVKrgARINIQDKQNHTALQYAVRGR 204
Cdd:cd21882   24 ATGKTCLHKAA---------------LNLNDGVNEAIMLLLEAAPDS--GNPKELVN--APCTDEFYQGQTALHIAIENR 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 442626107 205 HTQMAKLLLERGARRLAS-----------------QHLLHLAVESNVKELVELLLQYG 245
Cdd:cd21882   85 NLNLVRLLVENGADVSARatgrffrkspgnlfyfgELPLSLAACTNQEEIVRLLLENG 142
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
 430-486 1.31e-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: 36.37  E-value: 1.31e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 442626107  430 QPRSLQSLARLEIRRSLLRCLQtrpevqerylptqersslgRIVDEFAIPATLKRYL 486
Cdd:pfam07525   1 TPRSLQHLCRLAIRRALGKRRL-------------------GAIDKLPLPPLLKDYL 38
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 126-155 1.92e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.64  E-value: 1.92e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 442626107   126 DGKTALHMAIESKCAESARLLLQTNININD 155
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
112-164 1.94e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.56  E-value: 1.94e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 442626107  112 LIKHG-ALVNAKTLsDGKTALHMAIESKCAESARLLLQTNININDTDDDGETPL 164
Cdd:pfam13857   1 LLEHGpIDLNRLDG-EGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 186-276 3.06e-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: 3.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107  186 INIQDKQNHTALQY-AVRGRHTQMAKLLLERGARRLASQHLLHLAVEsNVKELVELLLQY-----GESLSVWNLKNF--- 256
Cdd:TIGR00870  45 INCPDRLGRSALFVaAIENENLELTELLLNLSCRGAVGDTLLHAISL-EYVDAVEAILLHllaafRKSGPLELANDQyts 123

                          90       100
                  ....*....|....*....|....*.
gi 442626107  257 ------TPIMLAIHRGRHEMLEYLLN 276
Cdd:TIGR00870 124 eftpgiTALHLAAHRQNYEIVKLLLE 149
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 59-125 3.33e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 40.05  E-value: 3.33e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442626107  59 DADVATPLHYAAYWGHE-ECVRILLEHNAPINVLNNDGYAPLHLGAGFAGVTELLIKHGA-LVNAKTLS 125
Cdd:PHA02876 439 NKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAINIQNQYPLLIALEYHGIVNILLHYGAeLRDSRVLH 507
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 111-185 3.72e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 38.32  E-value: 3.72e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442626107 111 LLIKHGALVNAKTLSDGKTALHMAIESKCAESARLLL-QTNININDTDDDGETPLMAAIACSMLDVAEELVKRGAR 185
Cdd:PHA02736  76 LLMEWGADINGKERVFGNTPLHIAVYTQNYELATWLCnQPGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGAQ 151
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 167-275 3.91e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 39.59  E-value: 3.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107 167 AIACSMLDVAEELVKRGARINIQDKQNHTALQYAVRGRHTQMAKLLLERGA----RRLASQHLLHLAVESNVKELVELLL 242
Cdd:PHA02875   9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAipdvKYPDIESELHDAVEEGDVKAVEELL 88

                         90       100       110
                 ....*....|....*....|....*....|....
gi 442626107 243 QYGESLS-VWNLKNFTPIMLAIHRGRHEMLEYLL 275
Cdd:PHA02875  89 DLGKFADdVFYKDGMTPLHLATILKKLDIMKLLI 122
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 126-158 4.61e-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: 4.61e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 442626107  126 DGKTALHMAIES-KCAESARLLLQTNININDTDD 158
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
SOCS_ASB_like cd03716
SOCS (suppressors of cytokine signaling) box of ASB (ankyrin repeat and SOCS box) and SSB ...
 430-486 4.84e-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: 34.78  E-value: 4.84e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 442626107 430 QPRSLQSLARLEIRrsllRCLQTRPEVQerylptqersslgriVDEFAIPATLKRYL 486
Cdd:cd03716    2 TPRSLQHLCRLAIR----RCLGRRRLEL---------------IKKLPLPPRLKDYL 39
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 159-188 8.71e-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: 8.71e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 442626107   159 DGETPLMAAIACSMLDVAEELVKRGARINI 188
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 118-275 8.80e-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: 38.71  E-value: 8.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107 118 LVNAKTLSD---GKTALHMAIESKCAESARLLLQTNININDTDDD-------------GETPLMAAIACSMLDVAEELVK 181
Cdd:cd21882   61 LVNAPCTDEfyqGQTALHIAIENRNLNLVRLLVENGADVSARATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLE 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107 182 RGARI---NIQDKQNHTALQYAV---------RGRHTQMAKLLLERGARrlaSQHLLHLavesnvkELVElllqygesls 249
Cdd:cd21882  141 NGAQPaalEAQDSLGNTVLHALVlqadntpenSAFVCQMYNLLLSYGAH---LDPTQQL-------EEIP---------- 200

                        170       180
                 ....*....|....*....|....*.
gi 442626107 250 vwNLKNFTPIMLAIHRGRHEMLEYLL 275
Cdd:cd21882  201 --NHQGLTPLKLAAVEGKIVMFQHIL 224
PHA02798 PHA02798
ankyrin-like protein; Provisional
 76-215 9.08e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 38.66  E-value: 9.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626107  76 ECVRILLEHNAPINVLNN-DGYAPLHLGAGF------AGVTELLIKHGALVNAKTLSDGKTALH----MAIESKCAESAR 144
Cdd:PHA02798 162 EIIKLLLEKGVDINTHNNkEKYDTLHCYFKYnidridADILKLFVDNGFIINKENKSHKKKFMEylnsLLYDNKRFKKNI 241

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442626107 145 L-LLQTNININDTDDDGETPLMAAIACSMLDVAEELVKRGARINIQDKQNHTALQYAVRGRHTQMAKLLLER 215
Cdd:PHA02798 242 LdFIFSYIDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNK 313
SOCS cd03587
SOCS (suppressors of cytokine signaling) box. The SOCS box is found in the C-terminal region ...
 430-486 9.43e-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: 33.98  E-value: 9.43e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 442626107 430 QPRSLQSLARLEIRrsllRCLQTRPEVQerylptqersslgriVDEFAIPATLKRYL 486
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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