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Conserved domains on  [gi|2462521182|ref|XP_054222806|]
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poly [ADP-ribose] polymerase tankyrase-2 isoform X5 [Homo sapiens]

Protein Classification

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

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
60-343 4.13e-44

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 157.04  E-value: 4.13e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182  60 TPLHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLLLRHGADPNARDNWNYTPLHEAAIKGKIDV 139
Cdd:COG0666    56 LLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 140 CIVLLQHGAEPTIRNTDGRtaldladpsakavltgeykkdellesarsgneekmmalltplnvnchasdgrksTPLHLAA 219
Cdd:COG0666   136 VKLLLEAGADVNAQDNDGN------------------------------------------------------TPLHLAA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 220 GYNRVKIVQLLLQHGADVHAKDKGDLVPLHNACSYGHYEVTELLVKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLLSY 299
Cdd:COG0666   162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 2462521182 300 GADPTLLNCHNKSAIDLAPTPQLKERLAYEFKGHSLLQAAREAD 343
Cdd:COG0666   242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
160-470 1.36e-37

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 139.32  E-value: 1.36e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 160 ALDLADPSAKAVLTGEYKKDELLESARSGNEEKMMALLTPLNVNCHASDGRKSTPLHLAAGYNRVKIVQLLLQHGADVHA 239
Cdd:COG0666    36 LLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNA 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 240 KDKGDLVPLHNACSYGHYEVTELLVKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLLSYGADPTLLNCHNksaidlapt 319
Cdd:COG0666   116 RDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDG--------- 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 320 pqlkerlayefkghsllqaareadvtrikkhlslemvnfkhpqthETALHCAAASpypKRKQICELLLRKGANINEKTKE 399
Cdd:COG0666   187 ---------------------------------------------ETPLHLAAEN---GHLEIVKLLLEAGADVNAKDND 218

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462521182 400 FLTPLHVASEKAHNDVVEVVVKHEAKVNALDNLGQTSLHRAAYCGHLQTCRLLLSYGCDPNIISLQGFTAL 470
Cdd:COG0666   219 GKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
60-343 4.13e-44

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 157.04  E-value: 4.13e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182  60 TPLHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLLLRHGADPNARDNWNYTPLHEAAIKGKIDV 139
Cdd:COG0666    56 LLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 140 CIVLLQHGAEPTIRNTDGRtaldladpsakavltgeykkdellesarsgneekmmalltplnvnchasdgrksTPLHLAA 219
Cdd:COG0666   136 VKLLLEAGADVNAQDNDGN------------------------------------------------------TPLHLAA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 220 GYNRVKIVQLLLQHGADVHAKDKGDLVPLHNACSYGHYEVTELLVKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLLSY 299
Cdd:COG0666   162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 2462521182 300 GADPTLLNCHNKSAIDLAPTPQLKERLAYEFKGHSLLQAAREAD 343
Cdd:COG0666   242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
160-470 1.36e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 139.32  E-value: 1.36e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 160 ALDLADPSAKAVLTGEYKKDELLESARSGNEEKMMALLTPLNVNCHASDGRKSTPLHLAAGYNRVKIVQLLLQHGADVHA 239
Cdd:COG0666    36 LLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNA 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 240 KDKGDLVPLHNACSYGHYEVTELLVKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLLSYGADPTLLNCHNksaidlapt 319
Cdd:COG0666   116 RDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDG--------- 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 320 pqlkerlayefkghsllqaareadvtrikkhlslemvnfkhpqthETALHCAAASpypKRKQICELLLRKGANINEKTKE 399
Cdd:COG0666   187 ---------------------------------------------ETPLHLAAEN---GHLEIVKLLLEAGADVNAKDND 218

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462521182 400 FLTPLHVASEKAHNDVVEVVVKHEAKVNALDNLGQTSLHRAAYCGHLQTCRLLLSYGCDPNIISLQGFTAL 470
Cdd:COG0666   219 GKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 73-458 1.58e-30

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 125.18  E-value: 1.58e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182  73 VVEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLLLRHGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGAE--- 149
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNink 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 150 ------PTIRNTDGRTALDLADPSAKAVLTGEYKKDELLESARSGNEEKMMALLTPLNVNCHASDGRKSTPLHLAA--GY 221
Cdd:PHA02876  240 ndlsllKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAknGY 319

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 222 NRVKIvQLLLQHGADVHAKDKGDLVPLHNACSYGHYEVTEL-LVKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLLSYG 300
Cdd:PHA02876  320 DTENI-RTLIMLGADVNAADRLYITPLHQASTLDRNKDIVItLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYG 398

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 301 ADPTLLNchnksaidlaptpqlkerlayefkghsllqaareadvtrikkhlslemvnfkhpQTHETALHCA--AASPYPK 378
Cdd:PHA02876  399 ADIEALS------------------------------------------------------QKIGTALHFAlcGTNPYMS 424

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 379 RKQicelLLRKGANINEKTKEFLTPLHVASEK-AHNDVVEVVVKHEAKVNALDNLGQTSLHRAayCGHLQTCRLLLSYGC 457
Cdd:PHA02876  425 VKT----LIDRGANVNSKNKDLSTPLHYACKKnCKLDVIEMLLDNGADVNAINIQNQYPLLIA--LEYHGIVNILLHYGA 498


                  .
gi 2462521182 458 D 458
Cdd:PHA02876  499 E 499
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 207-472 5.33e-28

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 115.53  E-value: 5.33e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 207 SDGRKSTPLHLAAGYNRVKIVQLLLQHGADVHAKDKGDLVPLHNACSYGHY-----EVTELLVKHGACVNAMDLWQFTPL 281
Cdd:PHA03100   31 SYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPL 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 282 HEAASK--NRVEVCSLLLSYGADPTLLNCHNksaidlaptpqlkerlayefkghsllqaareadvtrikkhlslemvnfk 359
Cdd:PHA03100  111 LYAISKksNSYSIVEYLLDNGANVNIKNSDG------------------------------------------------- 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 360 hpqthETALHCAAASPYPKRKqICELLLRKGANINEKTKefltplhvasekahndvVEVVVKHEAKVNALDNLGQTSLHR 439
Cdd:PHA03100  142 -----ENLLHLYLESNKIDLK-ILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIKDVYGFTPLHY 198

                         250       260       270
                  ....*....|....*....|....*....|...
gi 2462521182 440 AAYCGHLQTCRLLLSYGCDPNIISLQGFTALQM 472
Cdd:PHA03100  199 AVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHI 231
Ank_2 pfam12796
Ankyrin repeats (3 copies);
62-154 2.04e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.55  E-value: 2.04e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182  62 LHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLLLRHgADPNARDNwNYTPLHEAAIKGKIDVCI 141
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 2462521182 142 VLLQHGAEPTIRN 154
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
368-461 1.13e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.07  E-value: 1.13e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 368 LHCAAASPYPkrkQICELLLRKGANINEKTKEFLTPLHVASEKAHNDVVEVVVKHeAKVNALDNlGQTSLHRAAYCGHLQ 447
Cdd:pfam12796   1 LHLAAKNGNL---ELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLE 75

                          90
                  ....*....|....
gi 2462521182 448 TCRLLLSYGCDPNI 461
Cdd:pfam12796  76 IVKLLLEKGADINV 89
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 28-164 1.30e-09

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: 60.41  E-value: 1.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182  28 LFEACRNGDVERVKRLVT------------------------------------PEKVNSRDT----AGRksTPLHFAAG 67
Cdd:cd22192    21 LLLAAKENDVQAIKKLLKcpscdlfqrgalgetalhvaalydnleaavvlmeaaPELVNEPMTsdlyQGE--TALHIAVV 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182  68 FGRKDVVEYLLQNGANVQ-ARDDG--------GLI-----PLHNACSFGHAEVVNLLLRHGADPNARDNWNYTPLHE-AA 132
Cdd:cd22192    99 NQNLNLVRELIARGADVVsPRATGtffrpgpkNLIyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHIlVL 178

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2462521182 133 IKGKIDVCIV---LLQHGAE------PTIRNTDGRTALDLA 164
Cdd:cd22192   179 QPNKTFACQMydlILSYDKEddlqplDLVPNNQGLTPFKLA 219
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 60-172 4.91e-08

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: 55.47  E-value: 4.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182  60 TPLHFAAGFGRKDVVEYLLQNGANVQARDDG--------------GLIPLHNACSFGHAEVVNLLLRHGADPNARDNWNY 125
Cdd:TIGR00870 130 TALHLAAHRQNYEIVKLLLERGASVPARACGdffvksqgvdsfyhGESPLNAAACLGSPSIVALLSEDPADILTADSLGN 209

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462521182 126 TPLHEAAIKGKID------VCIV---LLQHGAEP-------TIRNTDGRTALDLADPSAKAVL 172
Cdd:TIGR00870 210 TLLHLLVMENEFKaeyeelSCQMynfALSLLDKLrdskeleVILNHQGLTPLKLAAKEGRIVL 272
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 91-119 7.67e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.49  E-value: 7.67e-05
                           10        20
                   ....*....|....*....|....*....
gi 2462521182   91 GLIPLHNACSFGHAEVVNLLLRHGADPNA 119
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 335-459 1.19e-03

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 41.54  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 335 LLQAAREADVTRIKKHLSLEMVNFKHPQTH-ETALHCAAASpypKRKQICELLLRKGAN-INEK-TKEF---LTPLHVAS 408
Cdd:cd22192    21 LLLAAKENDVQAIKKLLKCPSCDLFQRGALgETALHVAALY---DNLEAAVVLMEAAPElVNEPmTSDLyqgETALHIAV 97

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462521182 409 EKAHNDVVEVVVKHEAKVNA-----------LDNL---GQTSLHRAAYCGHLQTCRLLLSYGCDP 459
Cdd:cd22192    98 VNQNLNLVRELIARGADVVSpratgtffrpgPKNLiyyGEHPLSFAACVGNEEIVRLLIEHGADI 162
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 433-461 9.28e-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: 33.72  E-value: 9.28e-03
                           10        20
                   ....*....|....*....|....*....
gi 2462521182  433 GQTSLHRAAYCGHLQTCRLLLSYGCDPNI 461
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
60-343 4.13e-44

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 157.04  E-value: 4.13e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182  60 TPLHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLLLRHGADPNARDNWNYTPLHEAAIKGKIDV 139
Cdd:COG0666    56 LLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 140 CIVLLQHGAEPTIRNTDGRtaldladpsakavltgeykkdellesarsgneekmmalltplnvnchasdgrksTPLHLAA 219
Cdd:COG0666   136 VKLLLEAGADVNAQDNDGN------------------------------------------------------TPLHLAA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 220 GYNRVKIVQLLLQHGADVHAKDKGDLVPLHNACSYGHYEVTELLVKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLLSY 299
Cdd:COG0666   162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 2462521182 300 GADPTLLNCHNKSAIDLAPTPQLKERLAYEFKGHSLLQAAREAD 343
Cdd:COG0666   242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
28-307 9.75e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 153.19  E-value: 9.75e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182  28 LFEACRNGDVERVKRLVTPEKVNSRDTAGRKSTPLHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHAEVV 107
Cdd:COG0666    57 LLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIV 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 108 NLLLRHGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGAEPTIRNTDGRtaldladpsakavltgeykkdellesars 187
Cdd:COG0666   137 KLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGE----------------------------- 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 188 gneekmmalltplnvnchasdgrksTPLHLAAGYNRVKIVQLLLQHGADVHAKDKGDLVPLHNACSYGHYEVTELLVKHG 267
Cdd:COG0666   188 -------------------------TPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2462521182 268 ACVNAMDLWQFTPLHEAASKNRVEVCSLLLSYGADPTLLN 307
Cdd:COG0666   243 ADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
28-245 3.73e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 143.56  E-value: 3.73e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182  28 LFEACRNGDVERVKRLVT-PEKVNSRDTAGRksTPLHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHAEV 106
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEaGADVNARDKDGE--TPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEI 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 107 VNLLLRHGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGAEPTIRNTDGRTALDLAdpsakavltgeykkdellesAR 186
Cdd:COG0666   169 VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLA--------------------AE 228

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462521182 187 SGNEEkMMALLTPLNVNCHASDGRKSTPLHLAAGYNRVKIVQLLLQHGADVHAKDKGDL 245
Cdd:COG0666   229 NGNLE-IVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLL 286
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
160-470 1.36e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 139.32  E-value: 1.36e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 160 ALDLADPSAKAVLTGEYKKDELLESARSGNEEKMMALLTPLNVNCHASDGRKSTPLHLAAGYNRVKIVQLLLQHGADVHA 239
Cdd:COG0666    36 LLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNA 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 240 KDKGDLVPLHNACSYGHYEVTELLVKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLLSYGADPTLLNCHNksaidlapt 319
Cdd:COG0666   116 RDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDG--------- 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 320 pqlkerlayefkghsllqaareadvtrikkhlslemvnfkhpqthETALHCAAASpypKRKQICELLLRKGANINEKTKE 399
Cdd:COG0666   187 ---------------------------------------------ETPLHLAAEN---GHLEIVKLLLEAGADVNAKDND 218

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462521182 400 FLTPLHVASEKAHNDVVEVVVKHEAKVNALDNLGQTSLHRAAYCGHLQTCRLLLSYGCDPNIISLQGFTAL 470
Cdd:COG0666   219 GKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
53-317 5.34e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 137.78  E-value: 5.34e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182  53 DTAGRKSTPLHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLLLRHGADPNARDNWNYTPLHEAA 132
Cdd:COG0666    16 LLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 133 IKGKIDVCIVLLQHGAEPTIRNTDGRTaldladpsakavltgeykkdellesarsgneekmmalltplnvnchasdgrks 212
Cdd:COG0666    96 RNGDLEIVKLLLEAGADVNARDKDGET----------------------------------------------------- 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 213 tPLHLAAGYNRVKIVQLLLQHGADVHAKDKGDLVPLHNACSYGHYEVTELLVKHGACVNAMDLWQFTPLHEAASKNRVEV 292
Cdd:COG0666   123 -PLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEI 201

                         250       260
                  ....*....|....*....|....*
gi 2462521182 293 CSLLLSYGADPTLLNCHNKSAIDLA 317
Cdd:COG0666   202 VKLLLEAGADVNAKDNDGKTALDLA 226
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
161-470 6.64e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 126.61  E-value: 6.64e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 161 LDLADPSAKAVLTGEYKKDELLESARSGNEEKMMALLTPLNVNCHASDGRKSTPLHLAAGYNRVKIVQLLLQHGADVHAK 240
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 241 DKGDLVPLHNACSYGHYEVTELLVKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLLSYGADPTLLNCHNksaidlaptp 320
Cdd:COG0666    84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDG---------- 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 321 qlkerlayefkghsllqaareadvtrikkhlslemvnfkhpqthETALHCAAASpypKRKQICELLLRKGANINEKTKEF 400
Cdd:COG0666   154 --------------------------------------------NTPLHLAAAN---GNLEIVKLLLEAGADVNARDNDG 186

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 401 LTPLHVASEKAHNDVVEVVVKHEAKVNALDNLGQTSLHRAAYCGHLQTCRLLLSYGCDPNIISLQGFTAL 470
Cdd:COG0666   187 ETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTAL 256
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 73-458 1.58e-30

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 125.18  E-value: 1.58e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182  73 VVEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLLLRHGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGAE--- 149
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNink 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 150 ------PTIRNTDGRTALDLADPSAKAVLTGEYKKDELLESARSGNEEKMMALLTPLNVNCHASDGRKSTPLHLAA--GY 221
Cdd:PHA02876  240 ndlsllKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAknGY 319

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 222 NRVKIvQLLLQHGADVHAKDKGDLVPLHNACSYGHYEVTEL-LVKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLLSYG 300
Cdd:PHA02876  320 DTENI-RTLIMLGADVNAADRLYITPLHQASTLDRNKDIVItLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYG 398

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 301 ADPTLLNchnksaidlaptpqlkerlayefkghsllqaareadvtrikkhlslemvnfkhpQTHETALHCA--AASPYPK 378
Cdd:PHA02876  399 ADIEALS------------------------------------------------------QKIGTALHFAlcGTNPYMS 424

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 379 RKQicelLLRKGANINEKTKEFLTPLHVASEK-AHNDVVEVVVKHEAKVNALDNLGQTSLHRAayCGHLQTCRLLLSYGC 457
Cdd:PHA02876  425 VKT----LIDRGANVNSKNKDLSTPLHYACKKnCKLDVIEMLLDNGADVNAINIQNQYPLLIA--LEYHGIVNILLHYGA 498


                  .
gi 2462521182 458 D 458
Cdd:PHA02876  499 E 499
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 207-472 5.33e-28

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 115.53  E-value: 5.33e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 207 SDGRKSTPLHLAAGYNRVKIVQLLLQHGADVHAKDKGDLVPLHNACSYGHY-----EVTELLVKHGACVNAMDLWQFTPL 281
Cdd:PHA03100   31 SYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPL 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 282 HEAASK--NRVEVCSLLLSYGADPTLLNCHNksaidlaptpqlkerlayefkghsllqaareadvtrikkhlslemvnfk 359
Cdd:PHA03100  111 LYAISKksNSYSIVEYLLDNGANVNIKNSDG------------------------------------------------- 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 360 hpqthETALHCAAASPYPKRKqICELLLRKGANINEKTKefltplhvasekahndvVEVVVKHEAKVNALDNLGQTSLHR 439
Cdd:PHA03100  142 -----ENLLHLYLESNKIDLK-ILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIKDVYGFTPLHY 198

                         250       260       270
                  ....*....|....*....|....*....|...
gi 2462521182 440 AAYCGHLQTCRLLLSYGCDPNIISLQGFTALQM 472
Cdd:PHA03100  199 AVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHI 231
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
191-472 2.18e-27

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 111.20  E-value: 2.18e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 191 EKMMALLTPLNVNCHASDGRKSTPLHLAAGYNRVKIVQLLLQHGADVHAKDKGDLVPLHNACSYGHYEVTELLVKHGACV 270
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 271 NAMDLWQFTPLHEAASKNRVEVCSLLLSYGADPTLLNchnksaidlaptpqlkerlayefkghsllqaareadvtrikkh 350
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARD------------------------------------------- 117

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 351 lslemvnfkhpQTHETALHCAAASpypKRKQICELLLRKGANINEKTKEFLTPLHVASEKAHNDVVEVVVKHEAKVNALD 430
Cdd:COG0666   118 -----------KDGETPLHLAAYN---GNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD 183

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 2462521182 431 NLGQTSLHRAAYCGHLQTCRLLLSYGCDPNIISLQGFTALQM 472
Cdd:COG0666   184 NDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDL 225
PHA03095 PHA03095
ankyrin-like protein; Provisional
 29-317 1.88e-25

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 108.57  E-value: 1.88e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182  29 FEACRNGDVERVKRLV-TPEKVNSRDTAGRksTPLHFAAGFG---RKDVVEYLLQNGANVQARDDGGLIPLH----NACS 100
Cdd:PHA03095   19 LLNASNVTVEEVRRLLaAGADVNFRGEYGK--TPLHLYLHYSsekVKDIVRLLLEAGADVNAPERCGFTPLHlylyNATT 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 101 fghAEVVNLLLRHGADPNARDNWNYTPLHeAAIKGK-IDVCIV--LLQHGAEPTIRNTDGRTALDLadpsakavltgeyk 177
Cdd:PHA03095   97 ---LDVIKLLIKAGADVNAKDKVGRTPLH-VYLSGFnINPKVIrlLLRKGADVNALDLYGMTPLAV-------------- 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 178 kdeLLESARSgnEEKMMALLTPLNVNCHASDGRKSTPLHLAAGY--NRVKIVQLLLQHGADVHAKDKGDLVPLHNACSYG 255
Cdd:PHA03095  159 ---LLKSRNA--NVELLRLLIDAGADVYAVDDRFRSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSMATGS 233

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462521182 256 HYEVTEL--LVKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLLSYGADPTLLNCHNKSAIDLA 317
Cdd:PHA03095  234 SCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLM 297
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 57-358 2.03e-25

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 108.21  E-value: 2.03e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182  57 RKSTPLHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHA-----EVVNLLLRHGADPNARDNWNYTPLHEA 131
Cdd:PHA03100   34 KPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYA 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 132 AIKGKIDVCIV--LLQHGAeptirntdgrtaldladpsakavltgeykkdellesarsgneekmmalltplNVNCHASDG 209
Cdd:PHA03100  114 ISKKSNSYSIVeyLLDNGA----------------------------------------------------NVNIKNSDG 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 210 RksTPLHLAAGYNRV--KIVQLLLQHGADVHAKDKgdlvplhnacsyghyevTELLVKHGACVNAMDLWQFTPLHEAASK 287
Cdd:PHA03100  142 E--NLLHLYLESNKIdlKILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYN 202

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462521182 288 NRVEVCSLLLSYGADPTLLNCHNKSAIDLAPTPQLKERLAyefkghSLLQAAreADVTRIKKHLSLEMVNF 358
Cdd:PHA03100  203 NNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFK------LLLNNG--PSIKTIIETLLYFKDKD 265
PHA03095 PHA03095
ankyrin-like protein; Provisional
 179-470 3.18e-24

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 105.11  E-value: 3.18e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 179 DELLESARSGNEEKMMALLTPLNVNChaSDGRKSTPLHLAAGYN---RVKIVQLLLQHGADVHAKDKGDLVPLH----NA 251
Cdd:PHA03095   17 DYLLNASNVTVEEVRRLLAAGADVNF--RGEYGKTPLHLYLHYSsekVKDIVRLLLEAGADVNAPERCGFTPLHlylyNA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 252 CSYghyEVTELLVKHGACVNAMDLWQFTPLHE-AASKN-RVEVCSLLLSYGADPTLLNCHNKSAIdlaptpqlkerlaye 329
Cdd:PHA03095   95 TTL---DVIKLLIKAGADVNAKDKVGRTPLHVyLSGFNiNPKVIRLLLRKGADVNALDLYGMTPL--------------- 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 330 fkgHSLLqaaREADVTrikkhlsLEMVNF-----KHPQT----HETALHCAAASPYPkRKQICELLLRKGANINEKTKEF 400
Cdd:PHA03095  157 ---AVLL---KSRNAN-------VELLRLlidagADVYAvddrFRSLLHHHLQSFKP-RARIVRELIRAGCDPAATDMLG 222

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462521182 401 LTPLHVAS--EKAHNDVVEVVVKHEAKVNALDNLGQTSLHRAAYCGHLQTCRLLLSYGCDPNIISLQGFTAL 470
Cdd:PHA03095  223 NTPLHSMAtgSSCKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 65-303 4.19e-21

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 95.44  E-value: 4.19e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182  65 AAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLLLRHGADPNARDNWNYTPLHEAAIKGKIdvcivll 144
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDV------- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 145 qhgaeptirntdgrtaldladpsaKAVltgeykkDELLESARSGNEekmmalltplnvnCHASDGrkSTPLHLAAGYNRV 224
Cdd:PHA02875   82 ------------------------KAV-------EELLDLGKFADD-------------VFYKDG--MTPLHLATILKKL 115

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462521182 225 KIVQLLLQHGADVHAKDKGDLVPLHNACSYGHYEVTELLVKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLLSYGADP 303
Cdd:PHA02875  116 DIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANI 194
Ank_2 pfam12796
Ankyrin repeats (3 copies);
62-154 2.04e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.55  E-value: 2.04e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182  62 LHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLLLRHgADPNARDNwNYTPLHEAAIKGKIDVCI 141
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 2462521182 142 VLLQHGAEPTIRN 154
Cdd:pfam12796  79 LLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
28-161 7.92e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 89.63  E-value: 7.92e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182  28 LFEACRNGDVERVKRLVtpEK---VNSRDTAGRksTPLHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHA 104
Cdd:COG0666   157 LHLAAANGNLEIVKLLL--EAgadVNARDNDGE--TPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNL 232

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462521182 105 EVVNLLLRHGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGAEPTIRNTDGRTAL 161
Cdd:COG0666   233 EIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
215-307 2.96e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.47  E-value: 2.96e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 215 LHLAAGYNRVKIVQLLLQHGADVHAKDKGDLVPLHNACSYGHYEVTELLVKHgACVNaMDLWQFTPLHEAASKNRVEVCS 294
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVN-LKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 2462521182 295 LLLSYGADPTLLN 307
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 61-329 7.08e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 89.17  E-value: 7.08e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182  61 PLHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLLLR------------------HGADPNA--- 119
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRsinkcsvfytlvaikdafNNRNVEIfki 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 120 ----RDNWNYT----PLHEAAIKGKIDVCIV--LLQHGAEPTIRNTD-GRTALDLADpsakavltgeykkdellesarSG 188
Cdd:PHA02878  120 iltnRYKNIQTidlvYIDKKSKDDIIEAEITklLLSYGADINMKDRHkGNTALHYAT---------------------EN 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 189 NEEKMMALLTPLNVNCHASDGRKSTPLHLAAGYNRVKIVQLLLQHGADVHAKDKGDLVPLHNACSY-GHYEVTELLVKHG 267
Cdd:PHA02878  179 KDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHG 258

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462521182 268 ACVNAMD-LWQFTPLHEAASKNRVevCSLLLSYGADPTLLNCHNKSAIDLAptpqLKERLAYE 329
Cdd:PHA02878  259 VDVNAKSyILGLTALHSSIKSERK--LKLLLEYGADINSLNSYKLTPLSSA----VKQYLCIN 315
Ank_2 pfam12796
Ankyrin repeats (3 copies);
28-121 8.37e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.23  E-value: 8.37e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182  28 LFEACRNGDVERVKRLVTPEK-VNSRDTAGRksTPLHFAAGFGRKDVVEYLLQNgANVQARDDgGLIPLHNACSFGHAEV 106
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGAdANLQDKNGR--TALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEI 76

                          90
                  ....*....|....*
gi 2462521182 107 VNLLLRHGADPNARD 121
Cdd:pfam12796  77 VKLLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 72-289 1.98e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 81.16  E-value: 1.98e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182  72 DVVEYLLQNGAN-VQARDDGGLIPLHNACSFGHAEVVNLLLRHGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGAE- 149
Cdd:PHA02874   15 EAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDt 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 150 -----PTIRNTDGRTALDladpSAKAVLTGEYKKDELLESARSGNEEKMMALLTPLNVNCHASDGRKSTPLHLAAGYNRV 224
Cdd:PHA02874   95 silpiPCIEKDMIKTILD----CGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFF 170

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462521182 225 KIVQLLLQHGADVHAKDKGDLVPLHNACSYGHYEVTELLVKHGACVNAMDLWQFTPLHEAASKNR 289
Cdd:PHA02874  171 DIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR 235
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 34-327 3.90e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 80.39  E-value: 3.90e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182  34 NGDVERVKRLVTPEKVNSRDTAGRKSTPLHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLLLRH 113
Cdd:PHA02874   11 SGDIEAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDN 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 114 GADP-----------------------NARDNWNYTPLHEAAIKGKIDVCIVLLQHGAEPTIRNTDGRTALDLADPSaka 170
Cdd:PHA02874   91 GVDTsilpipciekdmiktildcgidvNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKH--- 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 171 vltgeykkdellesarsgNEEKMMALLTPLNVNCHASDGRKSTPLHLAAGYNRVKIVQLLLQHGADVHAKDKGDLVPLHN 250
Cdd:PHA02874  168 ------------------NFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHN 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 251 ACSYGHyEVTELLVKHgACVNAMDLWQFTPLHEAASKN-RVEVCSLLLSYGADPTLLNCHNKSAIDLA-----PTPQLKE 324
Cdd:PHA02874  230 AIIHNR-SAIELLINN-ASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTAfkyinKDPVIKD 307


                  ...
gi 2462521182 325 RLA 327
Cdd:PHA02874  308 IIA 310
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 71-184 9.12e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 79.32  E-value: 9.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182  71 KDVVEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLLLRHGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGA-- 148
Cdd:PHA03100  172 KNRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPsi 251

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2462521182 149 ---EPTI-----RNTDGRTALDLADPSAKAVLT---GEYKKDELLES 184
Cdd:PHA03100  252 ktiIETLlyfkdKDLNTITKIKMLKKSIMYMFLldpGFYKNRKLIEN 298
Ank_2 pfam12796
Ankyrin repeats (3 copies);
368-461 1.13e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.07  E-value: 1.13e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 368 LHCAAASPYPkrkQICELLLRKGANINEKTKEFLTPLHVASEKAHNDVVEVVVKHeAKVNALDNlGQTSLHRAAYCGHLQ 447
Cdd:pfam12796   1 LHLAAKNGNL---ELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLE 75

                          90
                  ....*....|....
gi 2462521182 448 TCRLLLSYGCDPNI 461
Cdd:pfam12796  76 IVKLLLEKGADINV 89
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 214-481 2.43e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 78.00  E-value: 2.43e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 214 PLHLAAGYNRVKIVQLLLQHGADVHAKDKGDLVPLHNACSYGHYE-VTELLvkhgACVNAMDL-WQFTPLHEAASKNRVE 291
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLgMKEMI----RSINKCSVfYTLVAIKDAFNNRNVE 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 292 VCSLLLSYGADptllnchNKSAIDLAPTPQLKERLAYEFKGHSLLqAAREADVTRIKKHlslemvnfkhpqTHETALHCA 371
Cdd:PHA02878  116 IFKIILTNRYK-------NIQTIDLVYIDKKSKDDIIEAEITKLL-LSYGADINMKDRH------------KGNTALHYA 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 372 AASPypkRKQICELLLRKGANINEKTKEFLTPLHVASEKAHNDVVEVVVKHEAKVNALDNLGQTSLHRA-AYCGHLQTCR 450
Cdd:PHA02878  176 TENK---DQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILK 252

                         250       260       270
                  ....*....|....*....|....*....|....
gi 2462521182 451 LLLSYGCDPNIIS-LQGFTALQMG--NENVQQLL 481
Cdd:PHA02878  253 LLLEHGVDVNAKSyILGLTALHSSikSERKLKLL 286
PHA03095 PHA03095
ankyrin-like protein; Provisional
 217-472 2.76e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 77.76  E-value: 2.76e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 217 LAAGYNRVKIVQLLLQHGADVHAKDKGDLVPLHnacSYGHY------EVTELLVKHGACVNAMDLWQFTPLH-EAASKNR 289
Cdd:PHA03095   20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLH---LYLHYssekvkDIVRLLLEAGADVNAPERCGFTPLHlYLYNATT 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 290 VEVCSLLLSYGADptllnchnksaidlaptpqlkerlayefkghslLQAAREADVTRIKKHLSLEMVNFKhpqthetalh 369
Cdd:PHA03095   97 LDVIKLLIKAGAD---------------------------------VNAKDKVGRTPLHVYLSGFNINPK---------- 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 370 caaaspypkrkqICELLLRKGANINEKTKEFLTPLHV--ASEKAHNDVVEVVVKHEAKVNALDNLGQTSLHRaaycgHLQ 447
Cdd:PHA03095  134 ------------VIRLLLRKGADVNALDLYGMTPLAVllKSRNANVELLRLLIDAGADVYAVDDRFRSLLHH-----HLQ 196

                         250       260       270
                  ....*....|....*....|....*....|..
gi 2462521182 448 TCR-------LLLSYGCDPNIISLQGFTALQM 472
Cdd:PHA03095  197 SFKprarivrELIRAGCDPAATDMLGNTPLHS 228
Ank_2 pfam12796
Ankyrin repeats (3 copies);
95-241 2.88e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.92  E-value: 2.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182  95 LHNACSFGHAEVVNLLLRHGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGaeptirntdgrtaldladpsakavltg 174
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA--------------------------- 53

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462521182 175 eykkdellesarsgneekmmalltplNVNChasDGRKSTPLHLAAGYNRVKIVQLLLQHGADVHAKD 241
Cdd:pfam12796  54 --------------------------DVNL---KDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 30-298 9.94e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 76.07  E-value: 9.94e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182  30 EACRNGDVERVKRLVTPEKVNSRDTAGRKSTPLHFAAGFGRKdVVEYLLQNGANVQARD-DGGLIPLHNACSFGHAEVVN 108
Cdd:PHA02878  107 DAFNNRNVEIFKIILTNRYKNIQTIDLVYIDKKSKDDIIEAE-ITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTE 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 109 LLLRHGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGAEPTIRNTDGrtaldladpsakavltgeykkdellesarsg 188
Cdd:PHA02878  186 LLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCG------------------------------- 234

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 189 neekmmalltplnvnchasdgrkSTPLHLAAGY-NRVKIVQLLLQHGADVHAKDK-GDLVPLHnaCSYGHYEVTELLVKH 266
Cdd:PHA02878  235 -----------------------NTPLHISVGYcKDYDILKLLLEHGVDVNAKSYiLGLTALH--SSIKSERKLKLLLEY 289

                         250       260       270
                  ....*....|....*....|....*....|...
gi 2462521182 267 GACVNAMDLWQFTPLHEAASKNR-VEVCSLLLS 298
Cdd:PHA02878  290 GADINSLNSYKLTPLSSAVKQYLcINIGRILIS 322
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 110-471 6.51e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 74.33  E-value: 6.51e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 110 LLRHGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGAEpTIRNTDGR------------TALDLA-----------DP 166
Cdd:PHA02876   27 LHKHGANQCENESIPFTAIHQALQLRQIDIVEEIIQQNPE-LIYITDHKchstlhticiipNVMDIVisltldcdiilDI 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 167 SAKAVLTGEYKKDE----LLESARSGNE-----------------------EKMMA-LLTPLNVNCHASDGRKSTPLHLA 218
Cdd:PHA02876  106 KYASIILNKHKLDEacihILKEAISGNDihydkinesieymklikeriqqdELLIAeMLLEGGADVNAKDIYCITPIHYA 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 219 AGYNRVKIVQLLLQHGADVHAKDKGDLVPLHNACSYGHYEVTELLVKHGACVNAMDLwqftPLHEAASKNRVEVCSLLLS 298
Cdd:PHA02876  186 AERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNDL----SLLKAIRNEDLETSLLLYD 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 299 YGADPTLLN-CHNKSAIDLAPTPQLkERLAYEfkghsLLQAAREADVTRIKKhlslemvnfkhpqthETALHCAAASPYP 377
Cdd:PHA02876  262 AGFSVNSIDdCKNTPLHHASQAPSL-SRLVPK-----LLERGADVNAKNIKG---------------ETPLYLMAKNGYD 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 378 KRKqiCELLLRKGANINEKTKEFLTPLHVASEKAHN-DVVEVVVKHEAKVNALDNLGQTSLHRAAYCGHLQTCRLLLSYG 456
Cdd:PHA02876  321 TEN--IRTLIMLGADVNAADRLYITPLHQASTLDRNkDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYG 398

                         410
                  ....*....|....*
gi 2462521182 457 CDPNIISLQGFTALQ 471
Cdd:PHA02876  399 ADIEALSQKIGTALH 413
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 59-269 1.57e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 72.61  E-value: 1.57e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182  59 STPLHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLLLRHGADPNARDNWNYTPLHEAAIKGK-I 137
Cdd:PHA02878  169 NTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKdY 248

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 138 DVCIVLLQHGaeptirntdgrtaldlADPSAKAVLTGeykkdellesarsgneekmmalLTPLNVNCHASDgrkstplhl 217
Cdd:PHA02878  249 DILKLLLEHG----------------VDVNAKSYILG----------------------LTALHSSIKSER--------- 281

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462521182 218 aagynrvkIVQLLLQHGADVHAKDKGDLVPLHNAC-SYGHYEVTELLVKHGAC 269
Cdd:PHA02878  282 --------KLKLLLEYGADINSLNSYKLTPLSSAVkQYLCINIGRILISNICL 326
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 79-281 4.80e-13

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 71.44  E-value: 4.80e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182  79 QNGANVQARDDGGLIplhNACSFGHAEVVNLLLRHGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGAEPTIRNTDGR 158
Cdd:PLN03192  516 NGGEHDDPNMASNLL---TVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGN 592

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 159 TALdladpsAKAVLTGEYKKDELL-ESARSGNEEKMMALLtplnvnChasdgrkstplhLAAGYNRVKIVQLLLQHGADV 237
Cdd:PLN03192  593 TAL------WNAISAKHHKIFRILyHFASISDPHAAGDLL------C------------TAAKRNDLTAMKELLKQGLNV 648

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2462521182 238 HAKDKGDLVPLHNACSYGHYEVTELLVKHGACVNAMDLWQ-FTPL 281
Cdd:PLN03192  649 DSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDdFSPT 693
PHA02798 PHA02798
ankyrin-like protein; Provisional
 224-476 3.57e-12

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 68.32  E-value: 3.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 224 VKIVQLLLQHGADVHAKDKGDLVPL----HNACSYGH-YEVTELLVKHGACVNAMDLWQFTPLHEAASK---NRVEVCSL 295
Cdd:PHA02798   51 TDIVKLFINLGANVNGLDNEYSTPLctilSNIKDYKHmLDIVKILIENGADINKKNSDGETPLYCLLSNgyiNNLEILLF 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 296 LLSYGADPTLLNCHNKSAIDLaptpqlkerlayefkghsLLQAAREADVTRIKkhLSLEM---VNFKHPQTHETALHCAA 372
Cdd:PHA02798  131 MIENGADTTLLDKDGFTMLQV------------------YLQSNHHIDIEIIK--LLLEKgvdINTHNNKEKYDTLHCYF 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 373 ASPYPK-RKQICELLLRKGANINEKTK-------EFLTPLHVASEKAHNDVVEVVVKHeAKVNALDNLGQTSLHRAAYCG 444
Cdd:PHA02798  191 KYNIDRiDADILKLFVDNGFIINKENKshkkkfmEYLNSLLYDNKRFKKNILDFIFSY-IDINQVDELGFNPLYYSVSHN 269

                         250       260       270
                  ....*....|....*....|....*....|..
gi 2462521182 445 HLQTCRLLLSYGCDPNIISLQGFTALQMGNEN 476
Cdd:PHA02798  270 NRKIFEYLLQLGGDINIITELGNTCLFTAFEN 301
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 60-306 3.84e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 68.09  E-value: 3.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182  60 TPLHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLLLRHG--ADPNARDNWNyTPLHEAAIKGKI 137
Cdd:PHA02875   37 SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGkfADDVFYKDGM-TPLHLATILKKL 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 138 DVCIVLLQHGAEPTIRNTDgrtaldladpsakavltgeykkdellesarsgneekmmalltplnvnchasdgrKSTPLHL 217
Cdd:PHA02875  116 DIMKLLIARGADPDIPNTD------------------------------------------------------KFSPLHL 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 218 AAGYNRVKIVQLLLQHGADVHAKDKGDLVPLHNACSYGHYEVTELLVKHGACVNAMDL-WQFTPLHEAASKNRVEVCSLL 296
Cdd:PHA02875  142 AVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKnGCVAALCYAIENNKIDIVRLF 221

                         250
                  ....*....|
gi 2462521182 297 LSYGADPTLL 306
Cdd:PHA02875  222 IKRGADCNIM 231
Ank_4 pfam13637
Ankyrin repeats (many copies);
59-111 4.38e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 60.75  E-value: 4.38e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462521182  59 STPLHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLLL 111
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 28-150 9.69e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 66.55  E-value: 9.69e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182  28 LFEACRNGDVERVKRLVTPEKVNSRDTAGRKSTPLHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHAEVV 107
Cdd:PHA02875   72 LHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGI 151

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2462521182 108 NLLLRHGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGAEP 150
Cdd:PHA02875  152 ELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANI 194
Ank_4 pfam13637
Ankyrin repeats (many copies);
212-264 1.82e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.13  E-value: 1.82e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462521182 212 STPLHLAAGYNRVKIVQLLLQHGADVHAKDKGDLVPLHNACSYGHYEVTELLV 264
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 53-164 3.90e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 62.19  E-value: 3.90e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182  53 DTAGRksTPLHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLL--LRHGADPNARDNWnytpLHE 130
Cdd:PLN03192  555 DSKGR--TPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILyhFASISDPHAAGDL----LCT 628

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2462521182 131 AAIKGKIDVCIVLLQHGAEPTIRNTDGRTALDLA 164
Cdd:PLN03192  629 AAKRNDLTAMKELLKQGLNVDSEDHQGATALQVA 662
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 102-167 6.19e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 61.45  E-value: 6.19e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462521182 102 GHAEVVNLLLRHGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGAEPTIRNTDGRTALDLADPS 167
Cdd:PTZ00322   93 GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEEN 158
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 28-268 7.40e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 61.23  E-value: 7.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182  28 LFEACRNG-DVERVKRLVT-PEKVNSRDTAgrKSTPLHFAAGFGR-KDVVEYLLQNGANVqarddggliplhnacsfgha 104
Cdd:PHA02876  311 LYLMAKNGyDTENIRTLIMlGADVNAADRL--YITPLHQASTLDRnKDIVITLLELGANV-------------------- 368

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 105 evvnlllrhgadpNARDNWNYTPLHEAAIKGKIDVCIVLLQHGAEPTIRNTDGRTALDLAdpsakavLTGEykkdelles 184
Cdd:PHA02876  369 -------------NARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFA-------LCGT--------- 419

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 185 arsgNEEKMMALLTPLNVNCHASDGRKSTPLHLAAGYN-RVKIVQLLLQHGADVHAKDKGDLVPLHNACSYghYEVTELL 263
Cdd:PHA02876  420 ----NPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIALEY--HGIVNIL 493


                  ....*
gi 2462521182 264 VKHGA 268
Cdd:PHA02876  494 LHYGA 498
PHA02946 PHA02946
ankyin-like protein; Provisional
 74-248 1.17e-09

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 60.45  E-value: 1.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182  74 VEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLLLRHGADPNARDNWNYTPLHeaAIKGKIDVCI----VLLQHGAE 149
Cdd:PHA02946   55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLY--YLSGTDDEVIerinLLVQYGAK 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 150 ptIRNTDGRTA----LDLADPSAK-----------AVLTGEYKKDELLESARSGN-EEKMMALLTPLNVNCHASDGRKST 213
Cdd:PHA02946  133 --INNSVDEEGcgplLACTDPSERvfkkimsigfeARIVDKFGKNHIHRHLMSDNpKASTISWMMKLGISPSKPDHDGNT 210

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2462521182 214 PLHLAAG--YNRVKIVQLLLQhGADVHAKDKGDLVPL 248
Cdd:PHA02946  211 PLHIVCSktVKNVDIINLLLP-STDVNKQNKFGDSPL 246
Ank_4 pfam13637
Ankyrin repeats (many copies);
247-297 1.28e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.82  E-value: 1.28e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462521182 247 PLHNACSYGHYEVTELLVKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLL 297
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 28-164 1.30e-09

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: 60.41  E-value: 1.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182  28 LFEACRNGDVERVKRLVT------------------------------------PEKVNSRDT----AGRksTPLHFAAG 67
Cdd:cd22192    21 LLLAAKENDVQAIKKLLKcpscdlfqrgalgetalhvaalydnleaavvlmeaaPELVNEPMTsdlyQGE--TALHIAVV 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182  68 FGRKDVVEYLLQNGANVQ-ARDDG--------GLI-----PLHNACSFGHAEVVNLLLRHGADPNARDNWNYTPLHE-AA 132
Cdd:cd22192    99 NQNLNLVRELIARGADVVsPRATGtffrpgpkNLIyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHIlVL 178

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2462521182 133 IKGKIDVCIV---LLQHGAE------PTIRNTDGRTALDLA 164
Cdd:cd22192   179 QPNKTFACQMydlILSYDKEddlqplDLVPNNQGLTPFKLA 219
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 247-481 1.43e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 59.98  E-value: 1.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 247 PLHNACSYGHYEVTELLVKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLLSYGADPTLLnchnksaidlaPTPQLKERL 326
Cdd:PHA02874   38 PLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSIL-----------PIPCIEKDM 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 327 AyefkgHSLLQAAREadvtrikkhlslemVNFKHPQThETALHCAAASpypKRKQICELLLRKGANINEKTKEFLTPLHV 406
Cdd:PHA02874  107 I-----KTILDCGID--------------VNIKDAEL-KTFLHYAIKK---GDLESIKMLFEYGADVNIEDDNGCYPIHI 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462521182 407 ASEKAHNDVVEVVVKHEAKVNALDNLGQTSLHRAAYCGHLQTCRLLLSYGCDPNIISLQGFTALQ---MGNENVQQLL 481
Cdd:PHA02874  164 AIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHnaiIHNRSAIELL 241
Ank_2 pfam12796
Ankyrin repeats (3 copies);
404-481 2.33e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 54.35  E-value: 2.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 404 LHVASEKAHNDVVEVVVKHEAKVNALDNLGQTSLHRAAYCGHLQTCRLLLSYgCDPNIISlQGFTAL----QMGNENVQQ 479
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALhyaaRSGHLEIVK 78


                  ..
gi 2462521182 480 LL 481
Cdd:pfam12796  79 LL 80
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 244-470 2.46e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 59.23  E-value: 2.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 244 DLVPLHNACSYGHYEVTELLVKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLLSYGADPTLlnchnksaidlaPTPQLK 323
Cdd:PHA02875    2 DQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDV------------KYPDIE 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 324 ERLAyefkghsllQAAREADVTRIKKHLSL-EMVNFKHPQTHETALHCAAASpypKRKQICELLLRKGANINEKTKEFLT 402
Cdd:PHA02875   70 SELH---------DAVEEGDVKAVEELLDLgKFADDVFYKDGMTPLHLATIL---KKLDIMKLLIARGADPDIPNTDKFS 137

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462521182 403 PLHVASEKAHNDVVEVVVKHEAKVNALDNLGQTSLHRAAYCGHLQTCRLLLSYGCDPNIISLQGFTAL 470
Cdd:PHA02875  138 PLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAA 205
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 162-269 2.47e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 59.53  E-value: 2.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 162 DLADPSAKAVLTGEykkdeLLESARSGNEEKMMALLTP-LNVNCHASDGRksTPLHLAAGYNRVKIVQLLLQHGADVHAK 240
Cdd:PTZ00322   72 EVIDPVVAHMLTVE-----LCQLAASGDAVGARILLTGgADPNCRDYDGR--TPLHIACANGHVQVVRVLLEFGADPTLL 144

                          90       100
                  ....*....|....*....|....*....
gi 2462521182 241 DKGDLVPLHNACSYGHYEVTELLVKHGAC 269
Cdd:PTZ00322  145 DKDGKTPLELAEENGFREVVQLLSRHSQC 173
Ank_5 pfam13857
Ankyrin repeats (many copies);
77-131 2.52e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 53.12  E-value: 2.52e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462521182  77 LLQNG-ANVQARDDGGLIPLHNACSFGHAEVVNLLLRHGADPNARDNWNYTPLHEA 131
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02798 PHA02798
ankyrin-like protein; Provisional
 72-306 2.68e-09

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 59.08  E-value: 2.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182  72 DVVEYLLQNGANVQARDDGGLIP----LHNACSFGHA-EVVNLLLRHGADPNARDNWNYTP----LHEAAIKGKiDVCIV 142
Cdd:PHA02798   52 DIVKLFINLGANVNGLDNEYSTPlctiLSNIKDYKHMlDIVKILIENGADINKKNSDGETPlyclLSNGYINNL-EILLF 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 143 LLQHGAEPTIRNTDGRTALDLadpsakAVLTGEYKKDELLEsarsgneekmMALLTPLNVNCHaSDGRKSTPLHLAAGYN 222
Cdd:PHA02798  131 MIENGADTTLLDKDGFTMLQV------YLQSNHHIDIEIIK----------LLLEKGVDINTH-NNKEKYDTLHCYFKYN 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 223 ----RVKIVQLLLQHGADVHAKDKGD-------LVPLHNACSYGHYEVTELLVKHgACVNAMDLWQFTPLHEAASKNRVE 291
Cdd:PHA02798  194 idriDADILKLFVDNGFIINKENKSHkkkfmeyLNSLLYDNKRFKKNILDFIFSY-IDINQVDELGFNPLYYSVSHNNRK 272

                         250
                  ....*....|....*
gi 2462521182 292 VCSLLLSYGADPTLL 306
Cdd:PHA02798  273 IFEYLLQLGGDINII 287
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 74-149 3.60e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 59.14  E-value: 3.60e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462521182  74 VEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLLLRHGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGAE 149
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQC 173
Ank_5 pfam13857
Ankyrin repeats (many copies);
110-164 5.52e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 51.96  E-value: 5.52e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462521182 110 LLRHG-ADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGAEPTIRNTDGRTALDLA 164
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
94-144 1.56e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.74  E-value: 1.56e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462521182  94 PLHNACSFGHAEVVNLLLRHGADPNARDNWNYTPLHEAAIKGKIDVCIVLL 144
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 216-299 2.85e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.45  E-value: 2.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 216 HLAAGYNRVKIvQLLLQHGADVHAKDKGDLVPLHNACSYGHYEVTELLVKHGACVNAMDLWQFTPLHEAASKNRVEVCSL 295
Cdd:PTZ00322   88 QLAASGDAVGA-RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                  ....
gi 2462521182 296 LLSY 299
Cdd:PTZ00322  167 LSRH 170
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 126-299 3.50e-08

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: 55.79  E-value: 3.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 126 TPLHEAAIKGKID-VCIVLLQHGAEPTIRNTDGRTALDLAdpsakaVLtgeYKKDE----LLESARsgneekmmallTPL 200
Cdd:cd22192    19 SPLLLAAKENDVQaIKKLLKCPSCDLFQRGALGETALHVA------AL---YDNLEaavvLMEAAP-----------ELV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 201 NVNCHASDGRKSTPLHLAAGYNRVKIVQLLLQHGADVHA---------KDKGDLV-----PLHNACSYGHYEVTELLVKH 266
Cdd:cd22192    79 NEPMTSDLYQGETALHIAVVNQNLNLVRELIARGADVVSpratgtffrPGPKNLIyygehPLSFAACVGNEEIVRLLIEH 158

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2462521182 267 GACVNAMDLWQFTPLH---EAASKNRV-EVCSLLLSY 299
Cdd:cd22192   159 GADIRAQDSLGNTVLHilvLQPNKTFAcQMYDLILSY 195
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 60-172 4.91e-08

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: 55.47  E-value: 4.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182  60 TPLHFAAGFGRKDVVEYLLQNGANVQARDDG--------------GLIPLHNACSFGHAEVVNLLLRHGADPNARDNWNY 125
Cdd:TIGR00870 130 TALHLAAHRQNYEIVKLLLERGASVPARACGdffvksqgvdsfyhGESPLNAAACLGSPSIVALLSEDPADILTADSLGN 209

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462521182 126 TPLHEAAIKGKID------VCIV---LLQHGAEP-------TIRNTDGRTALDLADPSAKAVL 172
Cdd:TIGR00870 210 TLLHLLVMENEFKaeyeelSCQMynfALSLLDKLrdskeleVILNHQGLTPLKLAAKEGRIVL 272
Ank_4 pfam13637
Ankyrin repeats (many copies);
401-453 7.62e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.81  E-value: 7.62e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462521182 401 LTPLHVASEKAHNDVVEVVVKHEAKVNALDNLGQTSLHRAAYCGHLQTCRLLL 453
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
335-430 1.27e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 49.34  E-value: 1.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 335 LLQAAREADVTRIKKHLSLEMVNFKHPQTHETALHCAAASpypKRKQICELLLRKgANINEKTKEFlTPLHVASEKAHND 414
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKN---GHLEIVKLLLEH-ADVNLKDNGR-TALHYAARSGHLE 75

                          90
                  ....*....|....*.
gi 2462521182 415 VVEVVVKHEAKVNALD 430
Cdd:pfam12796  76 IVKLLLEKGADINVKD 91
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 181-335 1.50e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.10  E-value: 1.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 181 LLESARSGN----EEKMMALLTPlnvncHASDGRKSTPLHLAAGYNRVKIVQLLLQHGADVHAKDKGDLVPLHNACSYGH 256
Cdd:PLN03192  529 LLTVASTGNaallEELLKAKLDP-----DIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKH 603

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 257 YEVTEL-------------------------------LVKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLLSYGADPTL 305
Cdd:PLN03192  604 HKIFRIlyhfasisdphaagdllctaakrndltamkeLLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDK 683

                         170       180       190
                  ....*....|....*....|....*....|
gi 2462521182 306 LNCHNksaiDLAPTpQLKERLAYEFKGHSL 335
Cdd:PLN03192  684 ANTDD----DFSPT-ELRELLQKRELGHSI 708
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 50-113 7.24e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.82  E-value: 7.24e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462521182  50 NSRDTAGRksTPLHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLLLRH 113
Cdd:PTZ00322  109 NCRDYDGR--TPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PHA03095 PHA03095
ankyrin-like protein; Provisional
 60-171 1.05e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 51.18  E-value: 1.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182  60 TPLHFAAGFG--RKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLLLRHGADPNARDNWNYTPLHEAAIKGki 137
Cdd:PHA03095  224 TPLHSMATGSscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNN-- 301

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2462521182 138 DVCIVllqhgaeptirntdgRTALDLAdPSAKAV 171
Cdd:PHA03095  302 NGRAV---------------RAALAKN-PSAETV 319
Ank_2 pfam12796
Ankyrin repeats (3 copies);
281-396 1.38e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 46.26  E-value: 1.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 281 LHEAASKNRVEVCSLLLSYGADPTLLNChnksaidlaptpqlkerlayefKGHSLLQAAREADVTRIKKHLsLEMVNFKH 360
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDK----------------------NGRTALHLAAKNGHLEIVKLL-LEHADVNL 57

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2462521182 361 PQTHETALHCAAASpypKRKQICELLLRKGANINEK 396
Cdd:pfam12796  58 KDNGRTALHYAARS---GHLEIVKLLLEKGADINVK 90
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 213-242 1.50e-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: 44.59  E-value: 1.50e-06
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2462521182 213 TPLHLAAG-YNRVKIVQLLLQHGADVHAKDK 242
Cdd:pfam00023   4 TPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
196-249 2.01e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.03  E-value: 2.01e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462521182 196 LLTPLNVNCHASDGRKSTPLHLAAGYNRVKIVQLLLQHGADVHAKDKGDLVPLH 249
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 213-301 8.52e-06

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 48.54  E-value: 8.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 213 TPLHLAAGYNRVKIVQLLLQHGADVHAKDKGDLV---PLHNACSYGHY-----------EVTELLVKHGACVNAMDLWQF 278
Cdd:TIGR00870 130 TALHLAAHRQNYEIVKLLLERGASVPARACGDFFvksQGVDSFYHGESplnaaaclgspSIVALLSEDPADILTADSLGN 209

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2462521182 279 TPLH------EAASKNRVEVCS---LLLSYGA 301
Cdd:TIGR00870 210 TLLHllvmenEFKAEYEELSCQmynFALSLLD 241
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 58-152 9.33e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 48.06  E-value: 9.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182  58 KSTPLHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLLLRHGADPN-ARDNWNYTPLHEAAIKGK 136
Cdd:PHA02875  135 KFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDyFGKNGCVAALCYAIENNK 214

                          90
                  ....*....|....*.
gi 2462521182 137 IDVCIVLLQHGAEPTI 152
Cdd:PHA02875  215 IDIVRLFIKRGADCNI 230
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 262-317 1.62e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.59  E-value: 1.62e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462521182 262 LLVKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLLSYGADPTLLNCHNKSAIDLA 317
Cdd:PTZ00322  100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA 155
Ank_4 pfam13637
Ankyrin repeats (many copies);
124-164 1.82e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.26  E-value: 1.82e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2462521182 124 NYTPLHEAAIKGKIDVCIVLLQHGAEPTIRNTDGRTALDLA 164
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFA 41
Ank_5 pfam13857
Ankyrin repeats (many copies);
263-317 1.87e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 1.87e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462521182 263 LVKHGAC-VNAMDLWQFTPLHEAASKNRVEVCSLLLSYGADPTLLNCHNKSAIDLA 317
Cdd:pfam13857   1 LLEHGPIdLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 91-122 1.88e-05

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. 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: 41.51  E-value: 1.88e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2462521182  91 GLIPLHNAC-SFGHAEVVNLLLRHGADPNARDN 122
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 60-172 2.18e-05

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 46.80  E-value: 2.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182  60 TPLHFAAGFGRKDVVEYLLQNGANVQARDDG-------------GLIPLHNACSFGHAEVVNLLLRHGADP---NARDNW 123
Cdd:cd21882    75 TALHIAIENRNLNLVRLLVENGADVSARATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPaalEAQDSL 154

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462521182 124 NYTPLH---EAAIKGKIDVCIV------LLQHGA--EPT-----IRNTDGRTALDLADPSAKAVL 172
Cdd:cd21882   155 GNTVLHalvLQADNTPENSAFVcqmynlLLSYGAhlDPTqqleeIPNHQGLTPLKLAAVEGKIVM 219
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 157-278 2.86e-05

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. 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.


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 46.72  E-value: 2.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 157 GRTALdladpsAKAVLTGEYKKDE----LLESARSGNEEKMMalltplnVNCHASDG--RKSTPLHLAAGYNRVKIVQLL 230
Cdd:cd22196    47 GKTCL------LKAMLNLHNGQNDtislLLDIAEKTGNLKEF-------VNAAYTDSyyKGQTALHIAIERRNMHLVELL 113

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2462521182 231 LQHGADVHAKDKGDLVPLhNACSYGHYeVTELLVKHGACVNAMDLWQF 278
Cdd:cd22196   114 VQNGADVHARASGEFFKK-KKGGPGFY-FGELPLSLAACTNQLDIVKF 159
Ank_5 pfam13857
Ankyrin repeats (many copies);
426-472 3.69e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.18  E-value: 3.69e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2462521182 426 VNALDNLGQTSLHRAAYCGHLQTCRLLLSYGCDPNIISLQGFTALQM 472
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 213-239 4.06e-05

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 40.32  E-value: 4.06e-05
                          10        20
                  ....*....|....*....|....*..
gi 2462521182 213 TPLHLAAGYNRVKIVQLLLQHGADVHA 239
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 60-89 4.34e-05

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. 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: 40.35  E-value: 4.34e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2462521182  60 TPLHFAAG-FGRKDVVEYLLQNGANVQARDD 89
Cdd:pfam00023   4 TPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
Ank_4 pfam13637
Ankyrin repeats (many copies);
435-481 4.58e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.11  E-value: 4.58e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462521182 435 TSLHRAAYCGHLQTCRLLLSYGCDPNIISLQGFTALQM----GNENVQQLL 481
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFaasnGNVEVLKLL 53
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 416-481 4.70e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.04  E-value: 4.70e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 416 VEVVVKHEAKVNALDNLGQTSLHRAAYCGHLQTCRLLLSYGCDPNIISLQGFTALQMGNEN----VQQLL 481
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENgfreVVQLL 167
Ank_5 pfam13857
Ankyrin repeats (many copies);
43-96 4.95e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.79  E-value: 4.95e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462521182  43 LVTPEKVNSRDTAGRKSTPLHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLH 96
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 105-308 5.72e-05

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 45.67  E-value: 5.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 105 EVVNLLLRHGADPNARDNWNYTPLHEAAIKGKIDVCIV--LLQHGAEPTIRNTDGRTaldladpsakAVLTgeykkdeLL 182
Cdd:PHA02716  193 DILEWLCNNGVNVNLQNNHLITPLHTYLITGNVCASVIkkIIELGGDMDMKCVNGMS----------PIMT-------YI 255

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 183 ESARSGNEEkmmalLTPLNVNCHASDGRKSTP--LHL---AAGYNRVKIVQLLLQHGADVHAKDKGDLVPLHNAC--SYG 255
Cdd:PHA02716  256 INIDNINPE-----ITNIYIESLDGNKVKNIPmiLHSyitLARNIDISVVYSFLQPGVKLHYKDSAGRTCLHQYIlrHNI 330

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462521182 256 HYEVTELLVKHGACVNAMDLWQFTPLH--------------EAASKNRVEVCSLLLSYGADPTLLNC 308
Cdd:PHA02716  331 STDIIKLLHEYGNDLNEPDNIGNTVLHtylsmlsvvnildpETDNDIRLDVIQCLISLGADITAVNC 397
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 91-119 7.67e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.49  E-value: 7.67e-05
                           10        20
                   ....*....|....*....|....*....
gi 2462521182   91 GLIPLHNACSFGHAEVVNLLLRHGADPNA 119
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 153-305 9.16e-05

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 44.87  E-value: 9.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 153 RNTDGRTALdladpsAKAVLTGEYKKDE----LLESARSGNEEKMMAlltplNVNCHASDGRKSTPLHLAAGYNRVKIVQ 228
Cdd:cd21882    22 RGATGKTCL------HKAALNLNDGVNEaimlLLEAAPDSGNPKELV-----NAPCTDEFYQGQTALHIAIENRNLNLVR 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 229 LLLQHGADVHAKDKGDL-------------VPLHNACSYGHYEVTELLVKHG---ACVNAMDLWQFTPLH---EAASK-- 287
Cdd:cd21882    91 LLVENGADVSARATGRFfrkspgnlfyfgeLPLSLAACTNQEEIVRLLLENGaqpAALEAQDSLGNTVLHalvLQADNtp 170

                         170       180
                  ....*....|....*....|....
gi 2462521182 288 -NRVEVCS---LLLSYGA--DPTL 305
Cdd:cd21882   171 eNSAFVCQmynLLLSYGAhlDPTQ 194
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 212-302 1.19e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 44.62  E-value: 1.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 212 STPLHLAAGYNRVKIVQ-LLLQHGADVHAKDKGDLVPLHNACSYGHYEVTELLVKhgaCV-----NAM--DLWQ-FTPLH 282
Cdd:cd22192    18 ESPLLLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME---AApelvnEPMtsDLYQgETALH 94

                          90       100
                  ....*....|....*....|
gi 2462521182 283 EAASKNRVEVCSLLLSYGAD 302
Cdd:cd22192    95 IAVVNQNLNLVRELIARGAD 114
PHA02946 PHA02946
ankyin-like protein; Provisional
 188-271 1.45e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 44.27  E-value: 1.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 188 GNEEKMMALLTPLNVNCHASDGRKSTPLHLAAGYNRVKIVQLLLQHGADVHAKDKGDLVPLHnACSYGHYEVTE---LLV 264
Cdd:PHA02946   49 GLDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLY-YLSGTDDEVIErinLLV 127


                  ....*..
gi 2462521182 265 KHGACVN 271
Cdd:PHA02946  128 QYGAKIN 134
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 49-186 1.79e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong 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: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 44.02  E-value: 1.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182  49 VNS--RDTAGRKSTPLHFAAGFGRKDVVEYLLQNGANVQARDDG--------------GLIPLHNACSFGHAEVVNLLLR 112
Cdd:cd22193    65 INAeyTDEYYEGQTALHIAIERRQGDIVALLVENGADVHAHAKGrffqpkyqgegfyfGELPLSLAACTNQPDIVQYLLE 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 113 HG---ADPNARDNWNYTPLH---EAAIKGKIDVCIV------LLQHGAE-------PTIRNTDGRTALDLADPSAKA--- 170
Cdd:cd22193   145 NEhqpADIEAQDSRGNTVLHalvTVADNTKENTKFVtrmydmILIRGAKlcptvelEEIRNNDGLTPLQLAAKMGKIeil 224

                         170
                  ....*....|....*...
gi 2462521182 171 --VLTGEYKKDELLESAR 186
Cdd:cd22193   225 kyILQREIKEPELRHLSR 242
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 213-239 1.91e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.72  E-value: 1.91e-04
                           10        20
                   ....*....|....*....|....*..
gi 2462521182  213 TPLHLAAGYNRVKIVQLLLQHGADVHA 239
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 384-452 2.08e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 44.09  E-value: 2.08e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462521182 384 ELLLRKGANINEKTKEFLTPLHVASEKAHNDVVEVVVKHEAKVNALDNLGQTSLHRAAYCGHLQTCRLL 452
Cdd:PLN03192  542 EELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610
Ank_5 pfam13857
Ankyrin repeats (many copies);
385-440 2.08e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.25  E-value: 2.08e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462521182 385 LLLRKGANINEKTKEFLTPLHVASEKAHNDVVEVVVKHEAKVNALDNLGQTSLHRA 440
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 213-310 2.19e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 42.50  E-value: 2.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 213 TPLH--LAAGYNRVKIVQLLLQHGADVHAKDKGD-LVPLHNACSYG---HYEVTELLVKHGACVNAMDLWQFTPLHEAAS 286
Cdd:PHA02859   53 TPIFscLEKDKVNVEILKFLIENGADVNFKTRDNnLSALHHYLSFNknvEPEILKILIDSGSSITEEDEDGKNLLHMYMC 132

                          90       100
                  ....*....|....*....|....*.
gi 2462521182 287 K--NRVEVCSLLLSYGADPTLLNCHN 310
Cdd:PHA02859  133 NfnVRINVIKLLIDSGVSFLNKDFDN 158
Ank_5 pfam13857
Ankyrin repeats (many copies);
230-284 2.88e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.87  E-value: 2.88e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462521182 230 LLQHG-ADVHAKDKGDLVPLHNACSYGHYEVTELLVKHGACVNAMDLWQFTPLHEA 284
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 47-169 3.44e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. 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.


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 43.26  E-value: 3.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182  47 EKVNS--RDTAGRKSTPLHFAAGFGRKDVVEYLLQNGANVQARDDG--------------GLIPLHNACSFGHAEVVNLL 110
Cdd:cd22196    81 EFVNAayTDSYYKGQTALHIAIERRNMHLVELLVQNGADVHARASGeffkkkkggpgfyfGELPLSLAACTNQLDIVKFL 160

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462521182 111 LRH---GADPNARDNWNYTPLH---EAAIKGKIDVCIV------LLQHGAE--PTIR-----NTDGRTALDLADPSAK 169
Cdd:cd22196   161 LENphsPADISARDSMGNTVLHalvEVADNTPENTKFVtkmyneILILGAKirPLLKleeitNKKGLTPLKLAAKTGK 238
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 94-119 5.21e-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: 5.21e-04
                          10        20
                  ....*....|....*....|....*.
gi 2462521182  94 PLHNACSFGHAEVVNLLLRHGADPNA 119
Cdd:pfam13606   5 PLHLAARNGRLEIVKLLLENGADINA 30
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 364-459 5.66e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 41.34  E-value: 5.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 364 HETALHCAAASPYPKrKQICELLLRKGANINEKTKEF-LTPLH---VASEKAHNDVVEVVVKHEAKVNALDNLGQTSLHR 439
Cdd:PHA02859   51 YETPIFSCLEKDKVN-VEILKFLIENGADVNFKTRDNnLSALHhylSFNKNVEPEILKILIDSGSSITEEDEDGKNLLHM 129

                          90       100
                  ....*....|....*....|....*..
gi 2462521182 440 aaycgHLQTC-------RLLLSYGCDP 459
Cdd:PHA02859  130 -----YMCNFnvrinviKLLIDSGVSF 151
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 60-86 5.75e-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: 5.75e-04
                          10        20
                  ....*....|....*....|....*..
gi 2462521182  60 TPLHFAAGFGRKDVVEYLLQNGANVQA 86
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADINA 30
PHA02743 PHA02743
Viral ankyrin protein; Provisional
 170-301 5.91e-04

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 40.57  E-value: 5.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 170 AVLTGEYKKDELLESARSGNEEKMMALLTPLNVNCHA-----SDGRKSTplHLAAGYNR---VKIVQLLLQHGADVHAKD 241
Cdd:PHA02743   13 AVEIDEDEQNTFLRICRTGNIYELMEVAPFISGDGHLlhrydHHGRQCT--HMVAWYDRanaVMKIELLVNMGADINARE 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462521182 242 K--GDLVpLHNACSYGHYEVTELLVKH-GACVNAMDLWQFTPLHEAASKNRVEVCSLLLSYGA 301
Cdd:PHA02743   91 LgtGNTL-LHIAASTKNYELAEWLCRQlGVNLGAINYQHETAYHIAYKMRDRRMMEILRANGA 152
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 384-481 8.57e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 41.52  E-value: 8.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 384 ELLLRKGANINEKTKEFLTPLHVASEKAHNDVVEVVVKHEAKVN-ALDNLGQTSLHRAAYCGHLQTCRLLLSYGCDPNII 462
Cdd:PHA02875   52 KLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIP 131

                          90       100
                  ....*....|....*....|...
gi 2462521182 463 SLQGFT----ALQMGNENVQQLL 481
Cdd:PHA02875  132 NTDKFSplhlAVMMGDIKGIELL 154
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 181-275 1.00e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 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 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.


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 41.76  E-value: 1.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 181 LLESARSGNEEKMmalltpLNVNCHASDGRKSTPLHLAAGYNRVKIVQLLLQHGADVHAKDKGDLVPLH-NACSYghyeV 259
Cdd:cd22197    70 LEIDKDSGNPKPL------VNAQCTDEYYRGHSALHIAIEKRSLQCVKLLVENGADVHARACGRFFQKKqGTCFY----F 139

                          90
                  ....*....|....*.
gi 2462521182 260 TELLVKHGACVNAMDL 275
Cdd:cd22197   140 GELPLSLAACTKQWDV 155
Ank_4 pfam13637
Ankyrin repeats (many copies);
364-417 1.06e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.25  E-value: 1.06e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462521182 364 HETALHCAAASPypkRKQICELLLRKGANINEKTKEFLTPLHVASEKAHNDVVE 417
Cdd:pfam13637   1 ELTALHAAAASG---HLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLK 51
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 335-459 1.19e-03

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 41.54  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 335 LLQAAREADVTRIKKHLSLEMVNFKHPQTH-ETALHCAAASpypKRKQICELLLRKGAN-INEK-TKEF---LTPLHVAS 408
Cdd:cd22192    21 LLLAAKENDVQAIKKLLKCPSCDLFQRGALgETALHVAALY---DNLEAAVVLMEAAPElVNEPmTSDLyqgETALHIAV 97

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462521182 409 EKAHNDVVEVVVKHEAKVNA-----------LDNL---GQTSLHRAAYCGHLQTCRLLLSYGCDP 459
Cdd:cd22192    98 VNQNLNLVRELIARGADVVSpratgtffrpgPKNLiyyGEHPLSFAACVGNEEIVRLLIEHGADI 162
PHA03095 PHA03095
ankyrin-like protein; Provisional
 385-477 1.43e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 41.16  E-value: 1.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 385 LLLRKGANINEKtKEFL-TPLHVASEKAHNDVVEVV---VKHEAKVNALDNLGQTSLHraAYCGHLQT---CRLLLSYGC 457
Cdd:PHA03095   32 RLLAAGADVNFR-GEYGkTPLHLYLHYSSEKVKDIVrllLEAGADVNAPERCGFTPLH--LYLYNATTldvIKLLIKAGA 108

                          90       100
                  ....*....|....*....|..
gi 2462521182 458 DPNIISLQGFTALQ--MGNENV 477
Cdd:PHA03095  109 DVNAKDKVGRTPLHvyLSGFNI 130
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 385-455 1.44e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.04  E-value: 1.44e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462521182 385 LLLRKGANINEKTKEFLTPLHVASEKAHNDVVEVVVKHEAKVNALDNLGQTSLHRAAYCGHLQTCRLLLSY 455
Cdd:PTZ00322  100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 41-170 1.44e-03

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: 41.28  E-value: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182  41 KRLVTPEKVNSrdtAGRKSTPLHFAAGFGRKDVVEYLLQNGANVQA-----------RDDG---GLIPLHNACSFGHAEV 106
Cdd:cd22194   127 DRFINAEYTEE---AYEGQTALNIAIERRQGDIVKLLIAKGADVNAhakgvffnpkyKHEGfyfGETPLALAACTNQPEI 203

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462521182 107 VNLLLRHGADPNA-RDNWNYTPLHEAAI-----KGKIDVCI-----VLLQHGAE--PTIRNTDGRTALDLADPSAKA 170
Cdd:cd22194   204 VQLLMEKESTDITsQDSRGNTVLHALVTvaedsKTQNDFVKrmydmILLKSENKnlETIRNNEGLTPLQLAAKMGKA 280
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 28-161 1.53e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 39.80  E-value: 1.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182  28 LFEACRNGDVERVKRLVTpekvNSRDTAGRKSTPLH--FAAGFGRKDVVEYLLQNGANVQARDDG-GLIPLHNACSFG-- 102
Cdd:PHA02859   25 LFYYVEKDDIEGVKKWIK----FVNDCNDLYETPIFscLEKDKVNVEILKFLIENGADVNFKTRDnNLSALHHYLSFNkn 100

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462521182 103 -HAEVVNLLLRHGADPNARDNWNYTPLHE--AAIKGKIDVCIVLLQHGAEPTIRNTDGRTAL 161
Cdd:PHA02859  101 vEPEILKILIDSGSSITEEDEDGKNLLHMymCNFNVRINVIKLLIDSGVSFLNKDFDNNNIL 162
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 61-145 1.66e-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: 41.22  E-value: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182  61 PLHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLH-----NACSFGHAEVV----NLLLRHGAD----------PNARD 121
Cdd:TIGR00870 178 PLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHllvmeNEFKAEYEELScqmyNFALSLLDKlrdskeleviLNHQG 257

                          90       100
                  ....*....|....*....|....
gi 2462521182 122 NwnyTPLHEAAIKGKIDVCIVLLQ 145
Cdd:TIGR00870 258 L---TPLKLAAKEGRIVLFRLKLA 278
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 60-84 1.68e-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: 1.68e-03
                           10        20
                   ....*....|....*....|....*
gi 2462521182   60 TPLHFAAGFGRKDVVEYLLQNGANV 84
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADI 28
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 346-428 2.28e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. 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.


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 40.56  E-value: 2.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 346 RIKKHLSLEmvNFKHPQTHETALHCAAASPYPKRKQICELLLrkgaNINEKT---KEFL------------TPLHVASEK 410
Cdd:cd22196    31 RTKKRLTDS--EFKDPETGKTCLLKAMLNLHNGQNDTISLLL----DIAEKTgnlKEFVnaaytdsyykgqTALHIAIER 104

                          90
                  ....*....|....*...
gi 2462521182 411 AHNDVVEVVVKHEAKVNA 428
Cdd:cd22196   105 RNMHLVELLVQNGADVHA 122
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 278-305 2.69e-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: 35.26  E-value: 2.69e-03
                           10        20
                   ....*....|....*....|....*...
gi 2462521182  278 FTPLHEAASKNRVEVCSLLLSYGADPTL 305
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 433-461 3.00e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.34  E-value: 3.00e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 2462521182 433 GQTSLHRAAY-CGHLQTCRLLLSYGCDPNI 461
Cdd:pfam00023   2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNA 31
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 200-303 3.34e-03

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: 40.13  E-value: 3.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521182 200 LNVNCHASDGRKSTPLHLAAGYNRVKIVQLLLQHGADVHAKDKGDLV-PLHNacsyghyevtellvkhgacvnaMDLWQF 278
Cdd:cd22194   130 INAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVFFnPKYK----------------------HEGFYF 187

                          90       100
                  ....*....|....*....|....*..
gi 2462521182 279 --TPLHEAASKNRVEVCSLLLSYGADP 303
Cdd:cd22194   188 geTPLALAACTNQPEIVQLLMEKESTD 214
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 365-398 4.24e-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: 4.24e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2462521182 365 ETALHCAAASPypKRKQICELLLRKGANINEKTK 398
Cdd:pfam00023   3 NTPLHLAAGRR--GNLEIVKLLLSKGADVNARDK 34
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 433-461 4.71e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.54  E-value: 4.71e-03
                          10        20
                  ....*....|....*....|....*....
gi 2462521182 433 GQTSLHRAAYCGHLQTCRLLLSYGCDPNI 461
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 62-130 4.73e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 39.47  E-value: 4.73e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462521182  62 LHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLLLRHGAD---PNARDNWNYTPLHE 130
Cdd:PLN03192  626 LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADvdkANTDDDFSPTELRE 697
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 124-152 5.24e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.49  E-value: 5.24e-03
                           10        20
                   ....*....|....*....|....*....
gi 2462521182  124 NYTPLHEAAIKGKIDVCIVLLQHGAEPTI 152
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 278-307 5.69e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.57  E-value: 5.69e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2462521182 278 FTPLHEAASK-NRVEVCSLLLSYGADPTLLN 307
Cdd:pfam00023   3 NTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 247-274 6.80e-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: 34.19  E-value: 6.80e-03
                          10        20
                  ....*....|....*....|....*....
gi 2462521182 247 PLHNAC-SYGHYEVTELLVKHGACVNAMD 274
Cdd:pfam00023   5 PLHLAAgRRGNLEIVKLLLSKGADVNARD 33
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 125-154 7.58e-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: 34.19  E-value: 7.58e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2462521182 125 YTPLHEAAIK-GKIDVCIVLLQHGAEPTIRN 154
Cdd:pfam00023   3 NTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 433-461 9.28e-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: 33.72  E-value: 9.28e-03
                           10        20
                   ....*....|....*....|....*....
gi 2462521182  433 GQTSLHRAAYCGHLQTCRLLLSYGCDPNI 461
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
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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