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Conserved domains on  [gi|442630835|ref|NP_001261537|]
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ankyrin 2, isoform X [Drosophila melanogaster]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 11430360)

ankyrin repeat (ANK) domain-containing protein 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

CATH:  1.25.40.20
Gene Ontology:  GO:0005515
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];
190-473 7.15e-46

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 162.82  E-value: 7.15e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 190 LLLDNDHNPDVTSKSGFTPLHIASHYGNQNIANLLIQKGADVNYSAKHNISPLHVAAKWGKTNMVSLLLEKGGNIEAKTR 269
Cdd:COG0666    6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 270 DGLTPLHCAARSGHEQVVDMLLERGAPISAKTKNGLAPLHMAAQGEHVDAARILLYHRAPVDEVTVDYLTALHVAAHCGH 349
Cdd:COG0666   86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 350 VRVAKLLLDRNADANARALNGFTPLHIACKKNRLKVVELLLRHGASISATTESGLTPLHVAAFMGCMNIVIYLLQHDASP 429
Cdd:COG0666  166 LEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADL 245
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 442630835 430 DVPTVRGETPLHLAARANQTDIIRILLRNGAQVDARAREQQTPL 473
Cdd:COG0666  246 NAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
10-308 3.42e-41

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 150.10  E-value: 3.42e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  10 DGNTSFLRAARAGNLERVLEHLKNNIDINTSNANGLNALHLASKDGHIHVVSELLRRGAIVDSATKKGNTALHIASLAGQ 89
Cdd:COG0666   20 LLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGD 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  90 EEVVKLLLEHNASVNVQSQNGFTPLYMAAQENHDAVVRLLLSNGANQSLATEDGFTPlavamqqghdkvvavllesdtrg 169
Cdd:COG0666  100 LEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTP----------------------- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 170 kvrlpaLHIAAKKDDVKAATLLLDNDHNPDVTSKSGFTPLHIASHYGNQNIANLLIQKGADVNYSAKHNISPLHVAAKWG 249
Cdd:COG0666  157 ------LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENG 230
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 442630835 250 KTNMVSLLLEKGGNIEAKTRDGLTPLHCAARSGHEQVVDMLLERGAPISAKTKNGLAPL 308
Cdd:COG0666  231 NLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
440-525 3.18e-15

Ankyrin repeats (3 copies);


:

Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.92  E-value: 3.18e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  440 LHLAARANQTDIIRILLRNGAQVDARAREQQTPLHIASRLGNVDIVMLLLQHgAQVDATTKDmYTALHIAAKEGQDE-VK 518
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG-RTALHYAARSGHLEiVK 78

                  ....*..
gi 442630835  519 DLIAKKI 525
Cdd:pfam12796  79 LLLEKGA 85
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
190-473 7.15e-46

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 162.82  E-value: 7.15e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 190 LLLDNDHNPDVTSKSGFTPLHIASHYGNQNIANLLIQKGADVNYSAKHNISPLHVAAKWGKTNMVSLLLEKGGNIEAKTR 269
Cdd:COG0666    6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 270 DGLTPLHCAARSGHEQVVDMLLERGAPISAKTKNGLAPLHMAAQGEHVDAARILLYHRAPVDEVTVDYLTALHVAAHCGH 349
Cdd:COG0666   86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 350 VRVAKLLLDRNADANARALNGFTPLHIACKKNRLKVVELLLRHGASISATTESGLTPLHVAAFMGCMNIVIYLLQHDASP 429
Cdd:COG0666  166 LEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADL 245
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 442630835 430 DVPTVRGETPLHLAARANQTDIIRILLRNGAQVDARAREQQTPL 473
Cdd:COG0666  246 NAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
10-308 3.42e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 150.10  E-value: 3.42e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  10 DGNTSFLRAARAGNLERVLEHLKNNIDINTSNANGLNALHLASKDGHIHVVSELLRRGAIVDSATKKGNTALHIASLAGQ 89
Cdd:COG0666   20 LLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGD 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  90 EEVVKLLLEHNASVNVQSQNGFTPLYMAAQENHDAVVRLLLSNGANQSLATEDGFTPlavamqqghdkvvavllesdtrg 169
Cdd:COG0666  100 LEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTP----------------------- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 170 kvrlpaLHIAAKKDDVKAATLLLDNDHNPDVTSKSGFTPLHIASHYGNQNIANLLIQKGADVNYSAKHNISPLHVAAKWG 249
Cdd:COG0666  157 ------LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENG 230
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 442630835 250 KTNMVSLLLEKGGNIEAKTRDGLTPLHCAARSGHEQVVDMLLERGAPISAKTKNGLAPL 308
Cdd:COG0666  231 NLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA03095 PHA03095
ankyrin-like protein; Provisional
219-489 3.15e-35

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 137.85  E-value: 3.15e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 219 NIANLLIQKGADVNYSAKHNISPLHVAAKWGK---TNMVSLLLEKGGNIEAKTRDGLTPLHCAARSGH-EQVVDMLLERG 294
Cdd:PHA03095  28 EEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAG 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 295 APISAKTKNGLAPLHMAAQGEHVDA--ARILLYHRAPVDEVTVDYLTALHV--AAHCGHVRVAKLLLDRNADANARALNG 370
Cdd:PHA03095 108 ADVNAKDKVGRTPLHVYLSGFNINPkvIRLLLRKGADVNALDLYGMTPLAVllKSRNANVELLRLLIDAGADVYAVDDRF 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 371 FTPLHIACK--KNRLKVVELLLRHGASISATTESGLTPLHVAA-FMGCMNIVIY-LLQHDASPDVPTVRGETPLHLAARA 446
Cdd:PHA03095 188 RSLLHHHLQsfKPRARIVRELIRAGCDPAATDMLGNTPLHSMAtGSSCKRSLVLpLLIAGISINARNRYGQTPLHYAAVF 267
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 442630835 447 NQTDIIRILLRNGAQVDARAREQQTPLHIASRLGNVDIVMLLL 489
Cdd:PHA03095 268 NNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
PHA03100 PHA03100
ankyrin repeat protein; Provisional
31-266 3.52e-30

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 122.47  E-value: 3.52e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  31 LKNNIDINTSNANGLNALHLASKDGHIHVVSELLRRGAIVDSATKKGNTALHIASLAGQE-----EVVKLLLEHNASVNV 105
Cdd:PHA03100  22 IMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNA 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 106 QSQNGFTPLYMAAQE--NHDAVVRLLLSNGANQSLATEDGFTPLAVAMQQGHD--KVVAVLLESDTrgkvrlpalHIAAK 181
Cdd:PHA03100 102 PDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGV---------DINAK 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 182 kDDVKaatLLLDNDHNPDVTSKSGFTPLHIASHYGNQNIANLLIQKGADVNYSAKHNISPLHVAAKWGKTNMVSLLLEKG 261
Cdd:PHA03100 173 -NRVN---YLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNG 248

                 ....*
gi 442630835 262 GNIEA 266
Cdd:PHA03100 249 PSIKT 253
Ank_2 pfam12796
Ankyrin repeats (3 copies);
341-431 2.52e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.86  E-value: 2.52e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  341 LHVAAHCGHVRVAKLLLDRNADANARALNGFTPLHIACKKNRLKVVELLLRHGAsiSATTESGLTPLHVAAFMGCMNIVI 420
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|.
gi 442630835  421 YLLQHDASPDV 431
Cdd:pfam12796  79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
48-135 1.19e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.93  E-value: 1.19e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835   48 LHLASKDGHIHVVSELLRRGAIVDSATKKGNTALHIASLAGQEEVVKLLLEHnASVNVQSqNGFTPLYMAAQENHDAVVR 127
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                  ....*...
gi 442630835  128 LLLSNGAN 135
Cdd:pfam12796  79 LLLEKGAD 86
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
112-313 2.57e-16

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: 81.98  E-value: 2.57e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 112 TPLYMAAQENH-DAVVRLLLSNGAnqslateDGFTplavamqqghdkvvavllesdtRGKVRLPALHIAAKKDDVKAATL 190
Cdd:cd22192   19 SPLLLAAKENDvQAIKKLLKCPSC-------DLFQ----------------------RGALGETALHVAALYDNLEAAVV 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 191 LLDNDH---NPDVTSK--SGFTPLHIASHYGNQNIANLLIQKGADVN-----------------YSAKHnisPLHVAAKW 248
Cdd:cd22192   70 LMEAAPelvNEPMTSDlyQGETALHIAVVNQNLNLVRELIARGADVVspratgtffrpgpknliYYGEH---PLSFAACV 146
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442630835 249 GKTNMVSLLLEKGGNIEAKTRDGLTPLHC----AARSGHEQVVDMLL-----ERGAPISAKTKN-GLAPLHMAAQ 313
Cdd:cd22192  147 GNEEIVRLLIEHGADIRAQDSLGNTVLHIlvlqPNKTFACQMYDLILsydkeDDLQPLDLVPNNqGLTPFKLAAK 221
Ank_2 pfam12796
Ankyrin repeats (3 copies);
440-525 3.18e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.92  E-value: 3.18e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  440 LHLAARANQTDIIRILLRNGAQVDARAREQQTPLHIASRLGNVDIVMLLLQHgAQVDATTKDmYTALHIAAKEGQDE-VK 518
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG-RTALHYAARSGHLEiVK 78

                  ....*..
gi 442630835  519 DLIAKKI 525
Cdd:pfam12796  79 LLLEKGA 85
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
263-456 2.34e-13

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: 72.81  E-value: 2.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  263 NIEAKTRDGLTPLHCAA-RSGHEQVVDMLLERGAPISAktknGLAPLHMAAQGEhVDAARILLYHRAPVDEVTVDY---- 337
Cdd:TIGR00870  44 NINCPDRLGRSALFVAAiENENLELTELLLNLSCRGAV----GDTLLHAISLEY-VDAVEAILLHLLAAFRKSGPLelan 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  338 ----------LTALHVAAHCGHVRVAKLLLDRNADANARALNGF--------------TPLHIACKKNRLKVVELLLRHG 393
Cdd:TIGR00870 119 dqytseftpgITALHLAAHRQNYEIVKLLLERGASVPARACGDFfvksqgvdsfyhgeSPLNAAACLGSPSIVALLSEDP 198
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442630835  394 ASISATTESGLTPLHVAAF------------MGCMNIVIYLLQHDASP----DVPTVRGETPLHLAARANQTDIIRILL 456
Cdd:TIGR00870 199 ADILTADSLGNTLLHLLVMenefkaeyeelsCQMYNFALSLLDKLRDSkeleVILNHQGLTPLKLAAKEGRIVLFRLKL 277
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
12-227 1.52e-11

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 66.96  E-value: 1.52e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  12 NTSFLRAARAGNLERVLEHLKNN-IDINTSNANGLNALHLASKDGHIHVVSELLR--RGAI---VDSATKKGNTALHIAS 85
Cdd:cd22192   18 ESPLLLAAKENDVQAIKKLLKCPsCDLFQRGALGETALHVAALYDNLEAAVVLMEaaPELVnepMTSDLYQGETALHIAV 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  86 LAGQEEVVKLLLEHNASVNVQSQNG--FT------------PLYMAAQENHDAVVRLLLSNGANqsLATED--GFTPLAV 149
Cdd:cd22192   98 VNQNLNLVRELIARGADVVSPRATGtfFRpgpknliyygehPLSFAACVGNEEIVRLLIEHGAD--IRAQDslGNTVLHI 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 150 AMQQGHDKVVA----VLLESDTRgkvrlpalhiaakkddvkaatlllDNDHNPD-VTSKSGFTPLHIASHYGNQNIANLL 224
Cdd:cd22192  176 LVLQPNKTFACqmydLILSYDKE------------------------DDLQPLDlVPNNQGLTPFKLAAKEGNIVMFQHL 231

                 ...
gi 442630835 225 IQK 227
Cdd:cd22192  232 VQK 234
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
441-530 3.77e-11

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 65.69  E-value: 3.77e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 441 HLAARANQTDIiRILLRNGAQVDARAREQQTPLHIASRLGNVDIVMLLLQHGAQVDATTKDMYTALHIAAKEGQDEVKDL 520
Cdd:PTZ00322  88 QLAASGDAVGA-RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166
                         90
                 ....*....|
gi 442630835 521 IAKKITDHID 530
Cdd:PTZ00322 167 LSRHSQCHFE 176
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
437-523 1.30e-07

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: 54.25  E-value: 1.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 437 ETPLHLAARANQTDIIRILLR-NGAQVDARAREQQTPLHIASRLGNVDIVMLLLQHGAQV--DATTKDMY---TALHIA- 509
Cdd:cd22192   18 ESPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELvnEPMTSDLYqgeTALHIAv 97
                         90
                 ....*....|....
gi 442630835 510 AKEGQDEVKDLIAK 523
Cdd:cd22192   98 VNQNLNLVRELIAR 111
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
11-248 3.76e-07

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 53.16  E-value: 3.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835   11 GNTSFLRAARAGNLERVLEHLKNNidiNTSNANGLNALHLASKdGHIHVVSELLR------RGA-----IVDSATK---K 76
Cdd:TIGR00870  52 GRSALFVAAIENENLELTELLLNL---SCRGAVGDTLLHAISL-EYVDAVEAILLhllaafRKSgplelANDQYTSeftP 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835   77 GNTALHIASLAGQEEVVKLLLEHNASVNV----------QSQNGF----TPLYMAAQENHDAVVRLLLSNGANQSLATED 142
Cdd:TIGR00870 128 GITALHLAAHRQNYEIVKLLLERGASVPAracgdffvksQGVDSFyhgeSPLNAAACLGSPSIVALLSEDPADILTADSL 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  143 GFTPLAVAMQQGHDKVVAVLLESdtrgKVRLPALHIAAKKDDVKAATLLLDNDhnpdvtsksGFTPLHIASHYGNQNIAN 222
Cdd:TIGR00870 208 GNTLLHLLVMENEFKAEYEELSC----QMYNFALSLLDKLRDSKELEVILNHQ---------GLTPLKLAAKEGRIVLFR 274
                         250       260       270
                  ....*....|....*....|....*....|
gi 442630835  223 LLIQkgadVNYSAK----HNISPLHVAAKW 248
Cdd:TIGR00870 275 LKLA----IKYKQKkfvaWPNGQQLLSLYW 300
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
369-398 1.21e-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: 42.19  E-value: 1.21e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 442630835   369 NGFTPLHIACKKNRLKVVELLLRHGASISA 398
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
76-105 9.43e-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: 9.43e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 442630835    76 KGNTALHIASLAGQEEVVKLLLEHNASVNV 105
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
471-497 5.46e-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: 5.46e-03
                           10        20
                   ....*....|....*....|....*..
gi 442630835   471 TPLHIASRLGNVDIVMLLLQHGAQVDA 497
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
190-473 7.15e-46

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 162.82  E-value: 7.15e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 190 LLLDNDHNPDVTSKSGFTPLHIASHYGNQNIANLLIQKGADVNYSAKHNISPLHVAAKWGKTNMVSLLLEKGGNIEAKTR 269
Cdd:COG0666    6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 270 DGLTPLHCAARSGHEQVVDMLLERGAPISAKTKNGLAPLHMAAQGEHVDAARILLYHRAPVDEVTVDYLTALHVAAHCGH 349
Cdd:COG0666   86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 350 VRVAKLLLDRNADANARALNGFTPLHIACKKNRLKVVELLLRHGASISATTESGLTPLHVAAFMGCMNIVIYLLQHDASP 429
Cdd:COG0666  166 LEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADL 245
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 442630835 430 DVPTVRGETPLHLAARANQTDIIRILLRNGAQVDARAREQQTPL 473
Cdd:COG0666  246 NAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
252-530 3.87e-45

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 160.89  E-value: 3.87e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 252 NMVSLLLEKGGNIEAKTRDGLTPLHCAARSGHEQVVDMLLERGAPISAKTKNGLAPLHMAAQGEHVDAARILLYHRAPVD 331
Cdd:COG0666    2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 332 EVTVDYLTALHVAAHCGHVRVAKLLLDRNADANARALNGFTPLHIACKKNRLKVVELLLRHGASISATTESGLTPLHVAA 411
Cdd:COG0666   82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 412 FMGCMNIVIYLLQHDASPDVPTVRGETPLHLAARANQTDIIRILLRNGAQVDARAREQQTPLHIASRLGNVDIVMLLLQH 491
Cdd:COG0666  162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 442630835 492 GAQVDATTKDMYTALHIAAKEGQDEVKDLIAKKITDHID 530
Cdd:COG0666  242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAA 280
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
219-506 1.15e-44

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 159.73  E-value: 1.15e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 219 NIANLLIQKGADVNYSAKHNISPLHVAAKWGKTNMVSLLLEKGGNIEAKTRDGLTPLHCAARSGHEQVVDMLLERGAPIS 298
Cdd:COG0666    2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 299 AKTKNGLAPLHMAAQGEHVDAARILLYHRAPVDEVTVDYLTALHVAAHCGHVRVAKLLLDRNADANARALNGFTPLHIAC 378
Cdd:COG0666   82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 379 KKNRLKVVELLLRHGASISATTESGLTPLHVAAFMGCMNIVIYLLQHDASPDVPTVRGETPLHLAARANQTDIIRILLRN 458
Cdd:COG0666  162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 442630835 459 GAQVDARAREQQTPLHIASRLGNVDIVMLLLQHGAQVDATTKDMYTAL 506
Cdd:COG0666  242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
175-427 1.37e-44

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 159.35  E-value: 1.37e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 175 ALHIAAKKDDVKAATLLLDNDHNPDVTSKSGFTPLHIASHYGNQNIANLLIQKGADVNYSAKHNISPLHVAAKWGKTNMV 254
Cdd:COG0666   24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIV 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 255 SLLLEKGGNIEAKTRDGLTPLHCAARSGHEQVVDMLLERGAPISAKTKNGLAPLHMAAQGEHVDAARILLYHRAPVDEVT 334
Cdd:COG0666  104 KLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 335 VDYLTALHVAAHCGHVRVAKLLLDRNADANARALNGFTPLHIACKKNRLKVVELLLRHGASISATTESGLTPLHVAAFMG 414
Cdd:COG0666  184 NDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAG 263
                        250
                 ....*....|...
gi 442630835 415 CMNIVIYLLQHDA 427
Cdd:COG0666  264 AALIVKLLLLALL 276
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
174-407 4.49e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 152.42  E-value: 4.49e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 174 PALHIAAKKDDVKAATLLLDNDHNPDVTSKSGFTPLHIASHYGNQNIANLLIQKGADVNYSAKHNISPLHVAAKWGKTNM 253
Cdd:COG0666   56 LLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 254 VSLLLEKGGNIEAKTRDGLTPLHCAARSGHEQVVDMLLERGAPISAKTKNGLAPLHMAAQGEHVDAARILLYHRAPVDEV 333
Cdd:COG0666  136 VKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAK 215
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442630835 334 TVDYLTALHVAAHCGHVRVAKLLLDRNADANARALNGFTPLHIACKKNRLKVVELLLRHGASISATTESGLTPL 407
Cdd:COG0666  216 DNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
10-308 3.42e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 150.10  E-value: 3.42e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  10 DGNTSFLRAARAGNLERVLEHLKNNIDINTSNANGLNALHLASKDGHIHVVSELLRRGAIVDSATKKGNTALHIASLAGQ 89
Cdd:COG0666   20 LLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGD 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  90 EEVVKLLLEHNASVNVQSQNGFTPLYMAAQENHDAVVRLLLSNGANQSLATEDGFTPlavamqqghdkvvavllesdtrg 169
Cdd:COG0666  100 LEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTP----------------------- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 170 kvrlpaLHIAAKKDDVKAATLLLDNDHNPDVTSKSGFTPLHIASHYGNQNIANLLIQKGADVNYSAKHNISPLHVAAKWG 249
Cdd:COG0666  157 ------LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENG 230
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 442630835 250 KTNMVSLLLEKGGNIEAKTRDGLTPLHCAARSGHEQVVDMLLERGAPISAKTKNGLAPL 308
Cdd:COG0666  231 NLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
24-341 2.14e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 148.18  E-value: 2.14e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  24 LERVLEHLKNNIDINTSNANGLNALHLASKDGHIHVVSELLRRGAIVDSATKKGNTALHIASLAGQEEVVKLLLEHNASV 103
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 104 NVQSQNGFTPLYMAAQENHDAVVRLLLSNGANQSLATEDGFTPlavamqqghdkvvavllesdtrgkvrlpaLHIAAKKD 183
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETP-----------------------------LHLAAYNG 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 184 DVKAATLLLDNDHNPDVTSKSGFTPLHIASHYGNQNIANLLIQKGADVNYSAKHNISPLHVAAKWGKTNMVSLLLEKGGN 263
Cdd:COG0666  132 NLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGAD 211
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442630835 264 IEAKTRDGLTPLHCAARSGHEQVVDMLLERGAPISAKTKNGLAPLHMAAQGEHVDAARILLYHRAPVDEVTVDYLTAL 341
Cdd:COG0666  212 VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA03095 PHA03095
ankyrin-like protein; Provisional
219-489 3.15e-35

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 137.85  E-value: 3.15e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 219 NIANLLIQKGADVNYSAKHNISPLHVAAKWGK---TNMVSLLLEKGGNIEAKTRDGLTPLHCAARSGH-EQVVDMLLERG 294
Cdd:PHA03095  28 EEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAG 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 295 APISAKTKNGLAPLHMAAQGEHVDA--ARILLYHRAPVDEVTVDYLTALHV--AAHCGHVRVAKLLLDRNADANARALNG 370
Cdd:PHA03095 108 ADVNAKDKVGRTPLHVYLSGFNINPkvIRLLLRKGADVNALDLYGMTPLAVllKSRNANVELLRLLIDAGADVYAVDDRF 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 371 FTPLHIACK--KNRLKVVELLLRHGASISATTESGLTPLHVAA-FMGCMNIVIY-LLQHDASPDVPTVRGETPLHLAARA 446
Cdd:PHA03095 188 RSLLHHHLQsfKPRARIVRELIRAGCDPAATDMLGNTPLHSMAtGSSCKRSLVLpLLIAGISINARNRYGQTPLHYAAVF 267
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 442630835 447 NQTDIIRILLRNGAQVDARAREQQTPLHIASRLGNVDIVMLLL 489
Cdd:PHA03095 268 NNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
5-197 1.57e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 132.00  E-value: 1.57e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835   5 NGAQGDGNTSFLRAARAGNLERVLEHLKNNIDINTSNANGLNALHLASKDGHIHVVSELLRRGAIVDSATKKGNTALHIA 84
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  85 SLAGQEEVVKLLLEHNASVNVQSQNGFTPLYMAAQENHDAVVRLLLSNGANQSLATEDGFTPLAVAMQQGHDKVVAVLLE 164
Cdd:COG0666  161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 442630835 165 S----DTRGKVRLPALHIAAKKDDVKAATLLLDNDHN 197
Cdd:COG0666  241 AgadlNAKDKDGLTALLLAAAAGAALIVKLLLLALLL 277
PHA03095 PHA03095
ankyrin-like protein; Provisional
115-407 5.17e-34

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 134.38  E-value: 5.17e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 115 YMAAQENHDA-VVRLLLSNGANQSLATEDGFTPLAVAMQQGHDKVVAVLLesdtrgkvrlpalhiaakkddvkaatLLLD 193
Cdd:PHA03095  18 YLLNASNVTVeEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIVR--------------------------LLLE 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 194 NDHNPDVTSKSGFTPLHIASHYGNQ-NIANLLIQKGADVNYSAKHNISPLHV--AAKWGKTNMVSLLLEKGGNIEAKTRD 270
Cdd:PHA03095  72 AGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLY 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 271 GLTPLHCAARSGHEQV--VDMLLERGAPISAKTKNGLAPLHMAAQGEHVDAARILLYHRAPVDEVTVDYL--TALHVAAH 346
Cdd:PHA03095 152 GMTPLAVLLKSRNANVelLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRARIVRELIRAGCDPAATDMLgnTPLHSMAT 231
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442630835 347 CGHVRVAKL--LLDRNADANARALNGFTPLHIACKKNRLKVVELLLRHGASISATTESGLTPL 407
Cdd:PHA03095 232 GSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294
PHA03100 PHA03100
ankyrin repeat protein; Provisional
224-464 1.95e-33

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 131.71  E-value: 1.95e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 224 LIQKGADVNYSAKHNISPLHVAAKWGKTNMVSLLLEKGGNIEAKTRDGLTPLHCAARSGHEQ-----VVDMLLERGAPIS 298
Cdd:PHA03100  21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLtdvkeIVKLLLEYGANVN 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 299 AKTKNGLAPLHMAAQG--EHVDAARILLYHRAPVDEVTVDYLTALHVAAHCGHV--RVAKLLLDRNADANAralngftpl 374
Cdd:PHA03100 101 APDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINA--------- 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 375 hiackKNRlkvVELLLRHGASISATTESGLTPLHVAAFMGCMNIVIYLLQHDASPDVPTVRGETPLHLAARANQTDIIRI 454
Cdd:PHA03100 172 -----KNR---VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKL 243
                        250
                 ....*....|
gi 442630835 455 LLRNGAQVDA 464
Cdd:PHA03100 244 LLNNGPSIKT 253
PHA02876 PHA02876
ankyrin repeat protein; Provisional
220-512 3.75e-33

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 134.04  E-value: 3.75e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 220 IANLLIQKGADVNYSAKHNISPLHVAAKWGKTNMVSLLLEKGGNIEAKTRDGLTPLHCAARSGHEQVVDMLLERGAPISa 299
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNIN- 238
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 300 ktKNGLAPLHmAAQGEHVDAARILLYHRAPVDEVTVDYLTALHVAAHCGHV-RVAKLLLDRNADANARALNGFTPLHIAC 378
Cdd:PHA02876 239 --KNDLSLLK-AIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMA 315
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 379 KKN-RLKVVELLLRHGASISATTESGLTPLHVAAFMG-CMNIVIYLLQHDASPDVPTVRGETPLHLAARANQTDIIRILL 456
Cdd:PHA02876 316 KNGyDTENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLL 395
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 442630835 457 RNGAQVDARAREQQTPLHIASRLGNVDI-VMLLLQHGAQVDATTKDMYTALHIAAKE 512
Cdd:PHA02876 396 DYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVNSKNKDLSTPLHYACKK 452
PHA02876 PHA02876
ankyrin repeat protein; Provisional
92-421 5.51e-32

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 130.57  E-value: 5.51e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  92 VVKLLLEHNASVNVQSQNGFTPLYMAAQENHDAVVRLLLSNGANQSLATEDGFTPLAVAMQQGH-DKVVAVLlesDTRGK 170
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNiDTIKAII---DNRSN 236
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 171 VRLPALHI--AAKKDDVKAATLLLDNDHNPDVTSKSGFTPLHIASHYGN-QNIANLLIQKGADVNYSAKHNISPLHVAAK 247
Cdd:PHA02876 237 INKNDLSLlkAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMAK 316
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 248 WG-KTNMVSLLLEKGGNIEAKTRDGLTPLHCAAR-SGHEQVVDMLLERGAPISAKTKNGLAPLHMAAQGEHVDAARILLY 325
Cdd:PHA02876 317 NGyDTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLD 396
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 326 HRAPVDEVTVDYLTALHVAAhCGH--VRVAKLLLDRNADANARALNGFTPLHIACKKN-RLKVVELLLRHGASISATTES 402
Cdd:PHA02876 397 YGADIEALSQKIGTALHFAL-CGTnpYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQ 475
                        330       340
                 ....*....|....*....|
gi 442630835 403 GLTPLHVA-AFMGCMNIVIY 421
Cdd:PHA02876 476 NQYPLLIAlEYHGIVNILLH 495
PHA03100 PHA03100
ankyrin repeat protein; Provisional
31-266 3.52e-30

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 122.47  E-value: 3.52e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  31 LKNNIDINTSNANGLNALHLASKDGHIHVVSELLRRGAIVDSATKKGNTALHIASLAGQE-----EVVKLLLEHNASVNV 105
Cdd:PHA03100  22 IMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNA 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 106 QSQNGFTPLYMAAQE--NHDAVVRLLLSNGANQSLATEDGFTPLAVAMQQGHD--KVVAVLLESDTrgkvrlpalHIAAK 181
Cdd:PHA03100 102 PDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGV---------DINAK 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 182 kDDVKaatLLLDNDHNPDVTSKSGFTPLHIASHYGNQNIANLLIQKGADVNYSAKHNISPLHVAAKWGKTNMVSLLLEKG 261
Cdd:PHA03100 173 -NRVN---YLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNG 248

                 ....*
gi 442630835 262 GNIEA 266
Cdd:PHA03100 249 PSIKT 253
PHA02876 PHA02876
ankyrin repeat protein; Provisional
181-495 8.67e-30

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 124.02  E-value: 8.67e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 181 KKDDVKAATLLLDNdhNPDVTSKSGF--TPLHIASHYGNQNIANLLIQKGADVNYSAKHNISPLHVAAKWGKTNMVSLLL 258
Cdd:PHA02876 154 QQDELLIAEMLLEG--GADVNAKDIYciTPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII 231
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 259 EKGGNIEAKTRDGL-----------------------------TPLHCAARSGH-EQVVDMLLERGAPISAKTKNGLAPL 308
Cdd:PHA02876 232 DNRSNINKNDLSLLkairnedletslllydagfsvnsiddcknTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPL 311
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 309 H-MAAQGEHVDAARILLYHRAPVDEVTVDYLTALHVAAHCGHVR-VAKLLLDRNADANARALNGFTPLHIACKKNRLKVV 386
Cdd:PHA02876 312 YlMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKdIVITLLELGANVNARDYCDKTPIHYAAVRNNVVII 391
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 387 ELLLRHGASISATTESGLTPLHVAAF-MGCMNIVIYLLQHDASPDVPTVRGETPLHLAARAN-QTDIIRILLRNGAQVDA 464
Cdd:PHA02876 392 NTLLDYGADIEALSQKIGTALHFALCgTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNA 471
                        330       340       350
                 ....*....|....*....|....*....|.
gi 442630835 465 RAREQQTPLHIAsrLGNVDIVMLLLQHGAQV 495
Cdd:PHA02876 472 INIQNQYPLLIA--LEYHGIVNILLHYGAEL 500
PHA03095 PHA03095
ankyrin-like protein; Provisional
59-332 1.89e-26

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 112.43  E-value: 1.89e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  59 VVSELLRRGAIVDSATKKGNTALHI-ASLAGQEEVVKLLLEHNASVNVQSQNGFTPL--YMAAQENHDAVVRLLLSNGAN 135
Cdd:PHA03095  65 IVRLLLEAGADVNAPERCGFTPLHLyLYNATTLDVIKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGAD 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 136 QSLATEDGFTPLAVAMQQGH--DKVVAVLLE--SDTRGK--VRLPALHIAAK--KDDVKAATLLLDNDHNPDVTSKSGFT 207
Cdd:PHA03095 145 VNALDLYGMTPLAVLLKSRNanVELLRLLIDagADVYAVddRFRSLLHHHLQsfKPRARIVRELIRAGCDPAATDMLGNT 224
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 208 PLHIASHYG---NQNIANLLIqKGADVNYSAKHNISPLHVAAKWGKTNMVSLLLEKGGNIEAKTRDGLTPLHCAARSGHE 284
Cdd:PHA03095 225 PLHSMATGSsckRSLVLPLLI-AGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNG 303
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442630835 285 QVVDMLLER------------------GAPISAKTKNGLAPLhMAAQGEHVDAARILLYHRAPVDE 332
Cdd:PHA03095 304 RAVRAALAKnpsaetvaatlntasvagGDIPSDATRLCVAKV-VLRGAFSLLPEPIRAYHADFIRE 368
PHA02874 PHA02874
ankyrin repeat protein; Provisional
55-330 6.44e-26

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 110.44  E-value: 6.44e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  55 GHIHVVSELLR-RGAIVDSATKKGNTALHIASLAGQEEVVKLLLEHNASVNVQSQNGFTPLYMAAQENHDAVVRLLLSNG 133
Cdd:PHA02874  12 GDIEAIEKIIKnKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 134 ANQSLatedgfTPLAVAMQQGHDKVVAVLLESDTRGKVRLPALHIAAKKDDVKAATLLLDNDHNPDVTSKSGFTPLHIAS 213
Cdd:PHA02874  92 VDTSI------LPIPCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAI 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 214 HYGNQNIANLLIQKGADVNYSAKHNISPLHVAAKWGKTNMVSLLLEKGGNIEAKTRDGLTPLHCAARsgHEQVVDMLLER 293
Cdd:PHA02874 166 KHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLIN 243
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 442630835 294 GAPISAKTKNGLAPLHMAAQGE-HVDAARILLYHRAPV 330
Cdd:PHA02874 244 NASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADI 281
PHA02874 PHA02874
ankyrin repeat protein; Provisional
90-410 1.01e-25

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 109.67  E-value: 1.01e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  90 EEVVKLLLEHNASVNVQSQNGFTPLYMAAQENHDAVVRLLLSNGANQSLATEDGFTPLAVAMQQGHDKVVAVLLESDTRG 169
Cdd:PHA02874  15 EAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDT 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 170 KVrLPALHIaaKKDDVKAatlLLDNDHNPDVTSKSGFTPLHIASHYGNQNIANLLIQKGADVNYSAKHNISPLHVAAKWG 249
Cdd:PHA02874  95 SI-LPIPCI--EKDMIKT---ILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHN 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 250 KTNMVSLLLEKGGNIEAKTRDGLTPLHCAARSGHEQVVDMLLERGAPISAKTKNGLAPLHMAaqgehvdaariLLYHRAP 329
Cdd:PHA02874 169 FFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA-----------IIHNRSA 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 330 VDevtvdyltalhvaahcghvrvaklLLDRNADANARALNGFTPLHIA----CKKNrlkVVELLLRHGASISATTESGLT 405
Cdd:PHA02874 238 IE------------------------LLINNASINDQDIDGSTPLHHAinppCDID---IIDILLYHKADISIKDNKGEN 290

                 ....*
gi 442630835 406 PLHVA 410
Cdd:PHA02874 291 PIDTA 295
PHA03095 PHA03095
ankyrin-like protein; Provisional
50-396 1.75e-25

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 109.34  E-value: 1.75e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  50 LASKDGHIHVVSELLRRGAIVDSATKKGNTALHI---ASLAGQEEVVKLLLEHNASVNVQSQNGFTPLYMAAQENHDA-V 125
Cdd:PHA03095  20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLylhYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdV 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 126 VRLLLSNGANQSLATEDGFTPLAVamqqghdkvvavllesdtrgkvrlpalHIAAKKDDVKAATLLLDNDHNPDVTSKSG 205
Cdd:PHA03095 100 IKLLIKAGADVNAKDKVGRTPLHV---------------------------YLSGFNINPKVIRLLLRKGADVNALDLYG 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 206 FTPLHI--ASHYGNQNIANLLIQKGADVNYSAKHNISPLHVAAKWGKTN--MVSLLLEKGGNIEAKTRDGLTPLHCAAR- 280
Cdd:PHA03095 153 MTPLAVllKSRNANVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMATg 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 281 -SGHEQVVDMLLERGAPISAKTKNGLAPLHMAAQGEHVDAARILLYHRAPVDEVTVDYLTALHVAAHCGHVRVAKLLLDR 359
Cdd:PHA03095 233 sSCKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAK 312
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 442630835 360 NADAN--ARALNGFTPLH--IACKKNRLKVVELLLRHGASI 396
Cdd:PHA03095 313 NPSAEtvAATLNTASVAGgdIPSDATRLCVAKVVLRGAFSL 353
PHA02878 PHA02878
ankyrin repeat protein; Provisional
272-514 6.35e-25

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 108.04  E-value: 6.35e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 272 LTPLHCAARSGHEQVVDMLLERGAPISAKTKNGLAPLHMAAQGEHVDAARILLyhrAPVDEVTVDY-LTALHVAAHCGHV 350
Cdd:PHA02878  38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMI---RSINKCSVFYtLVAIKDAFNNRNV 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 351 RVAKLLL----DRNADANARALngftplhiaCKKNR-----LKVVELLLRHGASISATTE-SGLTPLHVAAFMGCMNIVI 420
Cdd:PHA02878 115 EIFKIILtnryKNIQTIDLVYI---------DKKSKddiieAEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTE 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 421 YLLQHDASPDVPTVRGETPLHLAARANQTDIIRILLRNGAQVDARAREQQTPLHIA-SRLGNVDIVMLLLQHGAQVDATT 499
Cdd:PHA02878 186 LLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKS 265
                        250
                 ....*....|....*.
gi 442630835 500 KDM-YTALHIAAKEGQ 514
Cdd:PHA02878 266 YILgLTALHSSIKSER 281
PHA02878 PHA02878
ankyrin repeat protein; Provisional
111-436 3.28e-24

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 105.73  E-value: 3.28e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 111 FTPLYMAAQENHDAVVRLLLSNGANQSLATEDGFTPLAVAMQQGHDKVVAVLLESDTRGKV--RLPALHIAAKKDDVKAA 188
Cdd:PHA02878  38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVfyTLVAIKDAFNNRNVEIF 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 189 TLLLDNDHNPDVTSKSGFTPLHIASHYGNQNIANLLIQKGADVNYSAKHNI-SPLHVAAKWGKTNMVSLLLEKGGNIEAK 267
Cdd:PHA02878 118 KIILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDRHKGnTALHYATENKDQRLTELLLSYGANVNIP 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 268 TRDGLTPLHCAARSGHEQVVDMLLERGAPISAKTKNGLAPLHMAaqgehvdaarillyhrapvdevtvdyltalhvAAHC 347
Cdd:PHA02878 198 DKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIS--------------------------------VGYC 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 348 GHVRVAKLLLDRNADANARA-LNGFTPLHIACKKNRlkVVELLLRHGASISATTESGLTPLHVAAF----MGCMNIVIY- 421
Cdd:PHA02878 246 KDYDILKLLLEHGVDVNAKSyILGLTALHSSIKSER--KLKLLLEYGADINSLNSYKLTPLSSAVKqylcINIGRILISn 323
                        330
                 ....*....|....*.
gi 442630835 422 -LLQHDASPDVPTVRG 436
Cdd:PHA02878 324 iCLLKRIKPDIKNSEG 339
PHA02875 PHA02875
ankyrin repeat protein; Provisional
125-343 5.14e-24

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 104.30  E-value: 5.14e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 125 VVRLLLSNGANQSLATEDGFTPLAVAMQQGHDKVVAVLLESDTRGKVRLPA----LHIAAKKDDVKAATLLLD-NDHNPD 199
Cdd:PHA02875  17 IARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDieseLHDAVEEGDVKAVEELLDlGKFADD 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 200 VTSKSGFTPLHIASHYGNQNIANLLIQKGADVNYSAKHNISPLHVAAKWGKTNMVSLLLEKGGNIEAKTRDGLTPLHCAA 279
Cdd:PHA02875  97 VFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAM 176
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442630835 280 RSGHEQVVDMLLERGAPISAKTKNG-LAPLHMAAQGEHVDAARILLYHRAPVDEVTV---DYLTALHV 343
Cdd:PHA02875 177 AKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNIMFMiegEECTILDM 244
PHA02874 PHA02874
ankyrin repeat protein; Provisional
220-525 6.76e-23

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 101.19  E-value: 6.76e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 220 IANLLIQKGADVNYSAKHNISPLHVAAKWGKTNMVSLLLEKGGNIEAKTRDGLTPLHCAARSGHEQVVDMLLERGAPISa 299
Cdd:PHA02874  17 IEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTS- 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 300 ktkngLAPLHMAAQgehvDAARILLYHRAPVDEVTVDYLTALHVAAHCGHVRVAKLLLDRNADANARALNGFTPLHIACK 379
Cdd:PHA02874  96 -----ILPIPCIEK----DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIK 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 380 KNRLKVVELLLRHGASISATTESGLTPLHVAAFMGCMNIVIYLLQHDASPDVPTVRGETPLHLAARANQTDIirILLRNG 459
Cdd:PHA02874 167 HNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAI--ELLINN 244
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442630835 460 AQVDARAREQQTPLHIASRLG-NVDIVMLLLQHGAQVDATTKDMYTALHIAAKE-GQDEV-KDLIAKKI 525
Cdd:PHA02874 245 ASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTAFKYiNKDPViKDIIANAV 313
PHA02875 PHA02875
ankyrin repeat protein; Provisional
215-460 1.39e-22

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 100.07  E-value: 1.39e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 215 YGNQNIANLLIQKGADVNYSAKHNISPLHVAAKWGKTNMVSLLLEKGGNIEAKTRDGLTPLHCAARSGHEQVVDMLLERG 294
Cdd:PHA02875  12 FGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLG 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 295 APIS-AKTKNGLAPLHMAAQGEHVDAARILLYHRAPVDEVTVDYLTALHVAAHCGHVRVAKLLLDRNADANARALNGFTP 373
Cdd:PHA02875  92 KFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTP 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 374 LHIACKKNRLKVVELLLRHGASISATTESgltplhvaafmGCMNIVIYLLQHdaspdvptvrgetplhlaaraNQTDIIR 453
Cdd:PHA02875 172 LIIAMAKGDIAICKMLLDSGANIDYFGKN-----------GCVAALCYAIEN---------------------NKIDIVR 219

                 ....*..
gi 442630835 454 ILLRNGA 460
Cdd:PHA02875 220 LFIKRGA 226
PHA02878 PHA02878
ankyrin repeat protein; Provisional
81-344 2.04e-21

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 97.26  E-value: 2.04e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  81 LHIASLAGQEEVVKLLLEHNASVNVQSQNGFTPLYMAAQENHDAVVRLLLSNGANQSLatedGFTPLAVA-MQQGHDKVV 159
Cdd:PHA02878  41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSV----FYTLVAIKdAFNNRNVEI 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 160 AVLLESDTRGKVR---LPALHIAAKKDDVKAATLLLDNDHNPDVTSK---SGFTPLHIASHYGNQNIANLLIQKGADVNY 233
Cdd:PHA02878 117 FKIILTNRYKNIQtidLVYIDKKSKDDIIEAEITKLLLSYGADINMKdrhKGNTALHYATENKDQRLTELLLSYGANVNI 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 234 SAKHNISPLHVAAKWGKTNMVSLLLEKGGNIEAKTRDGLTPLHCA-ARSGHEQVVDMLLERGAPISAK-TKNGLAPLHMA 311
Cdd:PHA02878 197 PDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKsYILGLTALHSS 276
                        250       260       270
                 ....*....|....*....|....*....|...
gi 442630835 312 AQGEhvDAARILLYHRAPVDEVTVDYLTALHVA 344
Cdd:PHA02878 277 IKSE--RKLKLLLEYGADINSLNSYKLTPLSSA 307
PHA02875 PHA02875
ankyrin repeat protein; Provisional
278-502 2.29e-21

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 96.60  E-value: 2.29e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 278 AARSGHEQVVDMLLERGAPISAKTKNGLAPLHMAAQGEHVDAARILLYHRAPVDEVTVDYLTALHVAAHCGHVRVAKLLL 357
Cdd:PHA02875   9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 358 DRNADANARAL-NGFTPLHIACKKNRLKVVELLLRHGASISATTESGLTPLHVAAFMGCMNIVIYLLQHDASPDVPTVRG 436
Cdd:PHA02875  89 DLGKFADDVFYkDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCG 168
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442630835 437 ETPLHLAARANQTDIIRILLRNGAQVDARAREQQ-TPLHIASRLGNVDIVMLLLQHGAQVDATTKDM 502
Cdd:PHA02875 169 CTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADCNIMFMIE 235
PHA02874 PHA02874
ankyrin repeat protein; Provisional
31-248 3.54e-20

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 93.10  E-value: 3.54e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  31 LKNNIDINTSNANGLNALHLASKDGHIHVVSELLRRGAIVDSATKKGNTALHIASLAGQEEVVKLLLEHNASVNVQSQNG 110
Cdd:PHA02874 111 LDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNG 190
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 111 FTPLYMAAQENHDAVVRLLLSNGANQSLATEDGFTPLAVAMqqghdkvvavllesdtrgkvrlpaLHiaakkddVKAATL 190
Cdd:PHA02874 191 ESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI------------------------IH-------NRSAIE 239
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 442630835 191 LLDNDHNPDVTSKSGFTPLHIASHYG-NQNIANLLIQKGADVNYSAKHNISPLHVAAKW 248
Cdd:PHA02874 240 LLINNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTAFKY 298
Ank_2 pfam12796
Ankyrin repeats (3 copies);
341-431 2.52e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.86  E-value: 2.52e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  341 LHVAAHCGHVRVAKLLLDRNADANARALNGFTPLHIACKKNRLKVVELLLRHGAsiSATTESGLTPLHVAAFMGCMNIVI 420
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|.
gi 442630835  421 YLLQHDASPDV 431
Cdd:pfam12796  79 LLLEKGADINV 89
PHA02874 PHA02874
ankyrin repeat protein; Provisional
13-280 2.82e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 90.41  E-value: 2.82e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  13 TSFLRAARAGNLERVLEHLKNNIDINTSNANGLNALHLASKDGHIHVVSELLRRG-----------------AIVDSATK 75
Cdd:PHA02874  37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGvdtsilpipciekdmikTILDCGID 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  76 ------KGNTALHIASLAGQEEVVKLLLEHNASVNVQSQNGFTPLYMAAQENHDAVVRLLLSNGANQSLATEDGFTPlav 149
Cdd:PHA02874 117 vnikdaELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESP--- 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 150 amqqghdkvvavllesdtrgkvrlpaLHIAAKKDDVKAATLLLDNDHNPDVTSKSGFTPLHIASHYgNQNIANLLIQKgA 229
Cdd:PHA02874 194 --------------------------LHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIH-NRSAIELLINN-A 245
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 442630835 230 DVNYSAKHNISPLHVAAKWG-KTNMVSLLLEKGGNIEAKTRDGLTPLHCAAR 280
Cdd:PHA02874 246 SINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTAFK 297
Ank_2 pfam12796
Ankyrin repeats (3 copies);
308-399 5.60e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 81.70  E-value: 5.60e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  308 LHMAAQGEHVDAARILLYHRAPVDEVTVDYLTALHVAAHCGHVRVAKLLLDrNADANARaLNGFTPLHIACKKNRLKVVE 387
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLK-DNGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|..
gi 442630835  388 LLLRHGASISAT 399
Cdd:pfam12796  79 LLLEKGADINVK 90
PHA02875 PHA02875
ankyrin repeat protein; Provisional
22-263 7.37e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 88.89  E-value: 7.37e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  22 GNLERVLEHLKNNIDINTSNANGLNALHLASKDGHIHVVSELLRRGAIVDSATKKGNTALHIASLAGQEEVVKLLLEHNA 101
Cdd:PHA02875  13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 102 SVN-VQSQNGFTPLYMAAQENHDAVVRLLLSNGANQSLATEDGFTPlavamqqghdkvvavllesdtrgkvrlpaLHIAA 180
Cdd:PHA02875  93 FADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSP-----------------------------LHLAV 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 181 KKDDVKAATLLLDNDHNPDVTSKSGFTPLHIASHYGNQNIANLLIQKGADVNYSAKH-NISPLHVAAKWGKTNMVSLLLE 259
Cdd:PHA02875 144 MMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNgCVAALCYAIENNKIDIVRLFIK 223

                 ....
gi 442630835 260 KGGN 263
Cdd:PHA02875 224 RGAD 227
Ank_2 pfam12796
Ankyrin repeats (3 copies);
48-135 1.19e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.93  E-value: 1.19e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835   48 LHLASKDGHIHVVSELLRRGAIVDSATKKGNTALHIASLAGQEEVVKLLLEHnASVNVQSqNGFTPLYMAAQENHDAVVR 127
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                  ....*...
gi 442630835  128 LLLSNGAN 135
Cdd:pfam12796  79 LLLEKGAD 86
PHA03095 PHA03095
ankyrin-like protein; Provisional
339-508 1.37e-18

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 88.54  E-value: 1.37e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 339 TALHVAAHCGH---VRVAKLLLDRNADANARALNGFTPLHI-ACKKNRLKVVELLLRHGASISATTESGLTPLHVaafmg 414
Cdd:PHA03095  49 TPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLyLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHV----- 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 415 cmniviyllqhdaspdvptvrgetplHLAARANQTDIIRILLRNGAQVDARAREQQTPLHI--ASRLGNVDIVMLLLQHG 492
Cdd:PHA03095 124 --------------------------YLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVllKSRNANVELLRLLIDAG 177
                        170
                 ....*....|....*...
gi 442630835 493 AqvDATTKDMY--TALHI 508
Cdd:PHA03095 178 A--DVYAVDDRfrSLLHH 193
PHA02878 PHA02878
ankyrin repeat protein; Provisional
15-326 4.00e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 87.24  E-value: 4.00e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  15 FLRAARAGNLERVLEHLKNNIDINTSNANGLNALHLASKDGHIHVVSELLRR--GAIVDSATKKGNTALHIASLagqeEV 92
Cdd:PHA02878  41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSinKCSVFYTLVAIKDAFNNRNV----EI 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  93 VKLLLEHNASVNVQSQNGFTPLYMAAQENHDAVVRLLLSNGANQSLATEDGFTplavamqqghdkvvavllesdtrgkvr 172
Cdd:PHA02878 117 FKIILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDRHKGN--------------------------- 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 173 lPALHIAAKKDDVKAATLLLDNDHNPDVTSKSGFTPLHIASHYGNQNIANLLIQKGADVNYSAKHNISPLHVAAKWGKT- 251
Cdd:PHA02878 170 -TALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDy 248
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442630835 252 NMVSLLLEKGGNIEAK-TRDGLTPLHCAARSghEQVVDMLLERGAPISAKTKNGLAPLHMAA-QGEHVDAARILLYH 326
Cdd:PHA02878 249 DILKLLLEHGVDVNAKsYILGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSAVkQYLCINIGRILISN 323
Ank_2 pfam12796
Ankyrin repeats (3 copies);
15-106 5.43e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.00  E-value: 5.43e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835   15 FLRAARAGNLERVLEHLKNNIDINTSNANGLNALHLASKDGHIHVVSELLRRGAIvdSATKKGNTALHIASLAGQEEVVK 94
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|..
gi 442630835   95 LLLEHNASVNVQ 106
Cdd:pfam12796  79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
209-300 5.82e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.00  E-value: 5.82e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  209 LHIASHYGNQNIANLLIQKGADVNYSAKHNISPLHVAAKWGKTNMVSLLLEKGgNIEAKTrDGLTPLHCAARSGHEQVVD 288
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKD-NGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|..
gi 442630835  289 MLLERGAPISAK 300
Cdd:pfam12796  79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
407-498 6.67e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.62  E-value: 6.67e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  407 LHVAAFMGCMNIVIYLLQHDASPDVPTVRGETPLHLAARANQTDIIRILLRNgAQVDARArEQQTPLHIASRLGNVDIVM 486
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|..
gi 442630835  487 LLLQHGAQVDAT 498
Cdd:pfam12796  79 LLLEKGADINVK 90
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
112-313 2.57e-16

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: 81.98  E-value: 2.57e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 112 TPLYMAAQENH-DAVVRLLLSNGAnqslateDGFTplavamqqghdkvvavllesdtRGKVRLPALHIAAKKDDVKAATL 190
Cdd:cd22192   19 SPLLLAAKENDvQAIKKLLKCPSC-------DLFQ----------------------RGALGETALHVAALYDNLEAAVV 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 191 LLDNDH---NPDVTSK--SGFTPLHIASHYGNQNIANLLIQKGADVN-----------------YSAKHnisPLHVAAKW 248
Cdd:cd22192   70 LMEAAPelvNEPMTSDlyQGETALHIAVVNQNLNLVRELIARGADVVspratgtffrpgpknliYYGEH---PLSFAACV 146
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442630835 249 GKTNMVSLLLEKGGNIEAKTRDGLTPLHC----AARSGHEQVVDMLL-----ERGAPISAKTKN-GLAPLHMAAQ 313
Cdd:cd22192  147 GNEEIVRLLIEHGADIRAQDSLGNTVLHIlvlqPNKTFACQMYDLILsydkeDDLQPLDLVPNNqGLTPFKLAAK 221
Ank_2 pfam12796
Ankyrin repeats (3 copies);
81-166 2.62e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.00  E-value: 2.62e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835   81 LHIASLAGQEEVVKLLLEHNASVNVQSQNGFTPLYMAAQENHDAVVRLLLSNGANQSlaTEDGFTPLAVAMQQGHDKVVA 160
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78

                  ....*.
gi 442630835  161 VLLESD 166
Cdd:pfam12796  79 LLLEKG 84
Ank_2 pfam12796
Ankyrin repeats (3 copies);
176-267 2.76e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.00  E-value: 2.76e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  176 LHIAAKKDDVKAATLLLDNDHNPDVTSKSGFTPLHIASHYGNQNIANLLIQKgADVNYSAKHNiSPLHVAAKWGKTNMVS 255
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGR-TALHYAARSGHLEIVK 78
                          90
                  ....*....|..
gi 442630835  256 LLLEKGGNIEAK 267
Cdd:pfam12796  79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
242-328 7.66e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.84  E-value: 7.66e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  242 LHVAAKWGKTNMVSLLLEKGGNIEAKTRDGLTPLHCAARSGHEQVVDMLLERgaPISAKTKNGLAPLHMAAQGEHVDAAR 321
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH--ADVNLKDNGRTALHYAARSGHLEIVK 78

                  ....*..
gi 442630835  322 ILLYHRA 328
Cdd:pfam12796  79 LLLEKGA 85
PHA02875 PHA02875
ankyrin repeat protein; Provisional
336-523 2.97e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 77.72  E-value: 2.97e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 336 DYLTALHVAAHCGHVRVAKLLLDRNADANARALNGFTPLHIACKKNRLKVVELLLRHGASIS-ATTESGLTPLHVAAFMG 414
Cdd:PHA02875  34 DGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILK 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 415 CMNIVIYLLQHDASPDVPTVRGETPLHLAARANQTDIIRILLRNGAQVDARAREQQTPLHIASRLGNVDIVMLLLQHGAQ 494
Cdd:PHA02875 114 KLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGAN 193
                        170       180       190
                 ....*....|....*....|....*....|.
gi 442630835 495 VDATTKDMYTALHIAAKEGQ--DEVKDLIAK 523
Cdd:PHA02875 194 IDYFGKNGCVAALCYAIENNkiDIVRLFIKR 224
Ank_2 pfam12796
Ankyrin repeats (3 copies);
440-525 3.18e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.92  E-value: 3.18e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  440 LHLAARANQTDIIRILLRNGAQVDARAREQQTPLHIASRLGNVDIVMLLLQHgAQVDATTKDmYTALHIAAKEGQDE-VK 518
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG-RTALHYAARSGHLEiVK 78

                  ....*..
gi 442630835  519 DLIAKKI 525
Cdd:pfam12796  79 LLLEKGA 85
PHA02876 PHA02876
ankyrin repeat protein; Provisional
334-510 6.05e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 77.80  E-value: 6.05e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 334 TVDYLTALHVAAHCGHVRVAKLLLDRNADANARALNGFTPLHIACKKNRLKVVELLLRHGASISATTESGL--------- 404
Cdd:PHA02876 142 SIEYMKLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLsvlecavds 221
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 405 -----------------------------------------------------TPLHVAAFMGCMN-IVIYLLQHDASPD 430
Cdd:PHA02876 222 knidtikaiidnrsninkndlsllkairnedletslllydagfsvnsiddcknTPLHHASQAPSLSrLVPKLLERGADVN 301
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 431 VPTVRGETPLHLAAR-ANQTDIIRILLRNGAQVDARAREQQTPLHIASRLG-NVDIVMLLLQHGAQVDATTKDMYTALHI 508
Cdd:PHA02876 302 AKNIKGETPLYLMAKnGYDTENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHY 381

                 ..
gi 442630835 509 AA 510
Cdd:PHA02876 382 AA 383
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
263-456 2.34e-13

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: 72.81  E-value: 2.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  263 NIEAKTRDGLTPLHCAA-RSGHEQVVDMLLERGAPISAktknGLAPLHMAAQGEhVDAARILLYHRAPVDEVTVDY---- 337
Cdd:TIGR00870  44 NINCPDRLGRSALFVAAiENENLELTELLLNLSCRGAV----GDTLLHAISLEY-VDAVEAILLHLLAAFRKSGPLelan 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  338 ----------LTALHVAAHCGHVRVAKLLLDRNADANARALNGF--------------TPLHIACKKNRLKVVELLLRHG 393
Cdd:TIGR00870 119 dqytseftpgITALHLAAHRQNYEIVKLLLERGASVPARACGDFfvksqgvdsfyhgeSPLNAAACLGSPSIVALLSEDP 198
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442630835  394 ASISATTESGLTPLHVAAF------------MGCMNIVIYLLQHDASP----DVPTVRGETPLHLAARANQTDIIRILL 456
Cdd:TIGR00870 199 ADILTADSLGNTLLHLLVMenefkaeyeelsCQMYNFALSLLDKLRDSkeleVILNHQGLTPLKLAAKEGRIVLFRLKL 277
PHA02798 PHA02798
ankyrin-like protein; Provisional
34-293 2.62e-13

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 72.17  E-value: 2.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  34 NIDInTSNANGLNALHLASKDGHIHVVSELLRRGAIVDSATKKGNTAL-----HIASLAGQEEVVKLLLEHNASVNVQSQ 108
Cdd:PHA02798  29 NPNE-IVNEYSIFQKYLQRDSPSTDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNS 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 109 NGFTPLYMAAQE---NHDAVVRLLLSNGANQSLATEDGFTPLAVAMQQGHD---KVVAVLLESDT-----RGKVRLPALH 177
Cdd:PHA02798 108 DGETPLYCLLSNgyiNNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVdinthNNKEKYDTLH 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 178 IAAKKD----DVKAATLLLDND---HNPDVTSKSGFTPLHIASHYGNQNI-ANLL--IQKGADVNYSAKHNISPLHVAAK 247
Cdd:PHA02798 188 CYFKYNidriDADILKLFVDNGfiiNKENKSHKKKFMEYLNSLLYDNKRFkKNILdfIFSYIDINQVDELGFNPLYYSVS 267
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 442630835 248 WGKTNMVSLLLEKGGNIEAKTRDGLTPLHCAARSGHEQVVDMLLER 293
Cdd:PHA02798 268 HNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNK 313
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
307-513 2.92e-13

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: 72.35  E-value: 2.92e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 307 PLHMAAQGEHVDAARILL-------YHRAPVDEvtvdylTALHVAAHCGHVRVAKLLLDrnadaNARAL----------N 369
Cdd:cd22192   20 PLLLAAKENDVQAIKKLLkcpscdlFQRGALGE------TALHVAALYDNLEAAVVLME-----AAPELvnepmtsdlyQ 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 370 GFTPLHIACKKNRLKVVELLLRHGASISATTESGLtplhvaAFM-GCMNIVIYllqhdaspdvptvrGETPLHLAARANQ 448
Cdd:cd22192   89 GETALHIAVVNQNLNLVRELIARGADVVSPRATGT------FFRpGPKNLIYY--------------GEHPLSFAACVGN 148
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442630835 449 TDIIRILLRNGAQVDARAREQQTPLHIASRLGNVDIV--M--LLLQHGAQVDATTKDM------YTALHIAAKEG 513
Cdd:cd22192  149 EEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFAcqMydLILSYDKEDDLQPLDLvpnnqgLTPFKLAAKEG 223
PHA02989 PHA02989
ankyrin repeat protein; Provisional
218-490 4.04e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 71.70  E-value: 4.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 218 QNIANLLIQKGADVNYSAKHN-ISPLHVAAKWGKTNMVSLLLEKGGNIEAKtrdGL--TPLHCAAR------SGHEQVVD 288
Cdd:PHA02989  16 KNALEFLLRTGFDVNEEYRGNsILLLYLKRKDVKIKIVKLLIDNGADVNYK---GYieTPLCAVLRnreitsNKIKKIVK 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 289 MLLERGAPISAKTKNGLAPLHMAAQGEHV---DAARILLYHRAPVDEV-TVDYLTALHVAAHCGHVR--VAKLLLDRNAD 362
Cdd:PHA02989  93 LLLKFGADINLKTFNGVSPIVCFIYNSNInncDMLRFLLSKGINVNDVkNSRGYNLLHMYLESFSVKkdVIKILLSFGVN 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 363 A-NARALNGFTPLHIACKKN----RLKVVELLLRHGASISATT---ESGLTPL---HVAAFMGCMNIVIYLLQHdASPDV 431
Cdd:PHA02989 173 LfEKTSLYGLTPMNIYLRNDidviSIKVIKYLIKKGVNIETNNngsESVLESFldnNKILSKKEFKVLNFILKY-IKINK 251
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 442630835 432 PTVRGETPLHLAARANQTDIIRILLRNGAQVDARAREQQTPLHIASRLGNVDIVMLLLQ 490
Cdd:PHA02989 252 KDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLNRILQ 310
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
31-238 4.04e-13

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 72.21  E-value: 4.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  31 LKNNIDINTSNANGLNALHLASKdGHIHVVSELLRRGAIVDSATKKGNTALHIASLAGQEEVVKLLLEHNASVNVQSQNG 110
Cdd:PLN03192 513 LGDNGGEHDDPNMASNLLTVAST-GNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANG 591
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 111 FTPLYMAAQENHDAVVRLLLSnganqslatedgftplavamqqghdkvVAVLLESDTRGKVrlpaLHIAAKKDDVKAATL 190
Cdd:PLN03192 592 NTALWNAISAKHHKIFRILYH---------------------------FASISDPHAAGDL----LCTAAKRNDLTAMKE 640
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 442630835 191 LLDNDHNPDVTSKSGFTPLHIASHYGNQNIANLLIQKGADVNYSAKHN 238
Cdd:PLN03192 641 LLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDD 688
PHA02875 PHA02875
ankyrin repeat protein; Provisional
18-164 6.16e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 70.79  E-value: 6.16e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  18 AARAGNLERVLEHLKNNIDIN-TSNANGLNALHLASKDGHIHVVSELLRRGAIVDSATKKGNTALHIASLAGQEEVVKLL 96
Cdd:PHA02875  75 AVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELL 154
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442630835  97 LEHNASVNVQSQNGFTPLYMAAQENHDAVVRLLLSNGANQSLATEDG-FTPLAVAMQQGHDKVVAVLLE 164
Cdd:PHA02875 155 IDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIK 223
PHA03095 PHA03095
ankyrin-like protein; Provisional
31-165 6.20e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 70.82  E-value: 6.20e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  31 LKNNIDINTSNANGLNALH----------------------LASKDG------HIH---------VVSELLRRGAIVDSA 73
Cdd:PHA03095 139 LRKGADVNALDLYGMTPLAvllksrnanvellrllidagadVYAVDDrfrsllHHHlqsfkprarIVRELIRAGCDPAAT 218
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  74 TKKGNTALHIASLAGQEE--VVKLLLEHNASVNVQSQNGFTPLYMAAQENHDAVVRLLLSNGANQSLATEDGFTPLAVAM 151
Cdd:PHA03095 219 DMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMV 298
                        170
                 ....*....|....
gi 442630835 152 QQGHDKVVAVLLES 165
Cdd:PHA03095 299 RNNNGRAVRAALAK 312
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
356-532 1.83e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 70.28  E-value: 1.83e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 356 LLDRNADANARALNGFTPLHIACKKNRLKVVELLLRHGASISATTESGLTPLHVAAFMGcMNIVIYLLQHDASPDVPTVR 435
Cdd:PLN03192 544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAK-HHKIFRILYHFASISDPHAA 622
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 436 GETpLHLAARANQTDIIRILLRNGAQVDARAREQQTPLHIASRLGNVDIVMLLLQHGAQVD-ATTKDMYTALhiaakegq 514
Cdd:PLN03192 623 GDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDkANTDDDFSPT-------- 693
                        170
                 ....*....|....*...
gi 442630835 515 dEVKDLIAKKITDHIDTV 532
Cdd:PLN03192 694 -ELRELLQKRELGHSITI 710
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
106-324 9.06e-12

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: 67.80  E-value: 9.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  106 QSQNGFTPlymAAQENHDAVVRLLLSNGA--NQSLATEDGFTPLAVAMQQG-HDKVVAVLLESDTRGKVRLPALHIAAK- 181
Cdd:TIGR00870  16 DEEKAFLP---AAERGDLASVYRDLEEPKklNINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAVGDTLLHAISLe 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  182 -KDDVKAATLLLDNDHNPDVTSK-----------SGFTPLHIASHYGNQNIANLLIQKGADVNYSAK------------- 236
Cdd:TIGR00870  93 yVDAVEAILLHLLAAFRKSGPLElandqytseftPGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsf 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  237 -HNISPLHVAAKWGKTNMVSLLLEKGGNIEAKTRDGLTPLHCAA-----RSGHE----QVVDMLLERGAPISAKTK---- 302
Cdd:TIGR00870 173 yHGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVmenefKAEYEelscQMYNFALSLLDKLRDSKElevi 252
                         250       260
                  ....*....|....*....|....*
gi 442630835  303 ---NGLAPLHMAAQGEHVDAARILL 324
Cdd:TIGR00870 253 lnhQGLTPLKLAAKEGRIVLFRLKL 277
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
12-227 1.52e-11

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 66.96  E-value: 1.52e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  12 NTSFLRAARAGNLERVLEHLKNN-IDINTSNANGLNALHLASKDGHIHVVSELLR--RGAI---VDSATKKGNTALHIAS 85
Cdd:cd22192   18 ESPLLLAAKENDVQAIKKLLKCPsCDLFQRGALGETALHVAALYDNLEAAVVLMEaaPELVnepMTSDLYQGETALHIAV 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  86 LAGQEEVVKLLLEHNASVNVQSQNG--FT------------PLYMAAQENHDAVVRLLLSNGANqsLATED--GFTPLAV 149
Cdd:cd22192   98 VNQNLNLVRELIARGADVVSPRATGtfFRpgpknliyygehPLSFAACVGNEEIVRLLIEHGAD--IRAQDslGNTVLHI 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 150 AMQQGHDKVVA----VLLESDTRgkvrlpalhiaakkddvkaatlllDNDHNPD-VTSKSGFTPLHIASHYGNQNIANLL 224
Cdd:cd22192  176 LVLQPNKTFACqmydLILSYDKE------------------------DDLQPLDlVPNNQGLTPFKLAAKEGNIVMFQHL 231

                 ...
gi 442630835 225 IQK 227
Cdd:cd22192  232 VQK 234
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
1-163 3.66e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 66.04  E-value: 3.66e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835   1 MVTENGAQGDGNTSF--LRAARAGNLERVLEHLKNNIDINTSNANGLNALHLASKDGHIHVVSELLRRGAIVDSATKKGN 78
Cdd:PLN03192 513 LGDNGGEHDDPNMASnlLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGN 592
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  79 TALHIASLAGQEEVVKLLLeHNASVNvQSQNGFTPLYMAAQENHDAVVRLLLSNGANQSLATEDGFTPLAVAMQQGHDKV 158
Cdd:PLN03192 593 TALWNAISAKHHKIFRILY-HFASIS-DPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDM 670

                 ....*
gi 442630835 159 VAVLL 163
Cdd:PLN03192 671 VRLLI 675
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
441-530 3.77e-11

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 65.69  E-value: 3.77e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 441 HLAARANQTDIiRILLRNGAQVDARAREQQTPLHIASRLGNVDIVMLLLQHGAQVDATTKDMYTALHIAAKEGQDEVKDL 520
Cdd:PTZ00322  88 QLAASGDAVGA-RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166
                         90
                 ....*....|
gi 442630835 521 IAKKITDHID 530
Cdd:PTZ00322 167 LSRHSQCHFE 176
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
76-220 3.93e-11

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: 65.55  E-value: 3.93e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  76 KGNTALHIASLAGQEEVVKLLLEHNASVNVQSQNGF--------------TPLYMAAQENHDAVVRLLLSNGANQslate 141
Cdd:cd22194  140 EGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVFfnpkykhegfyfgeTPLALAACTNQPEIVQLLMEKESTD----- 214
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 142 dgftplaVAMQqghdkvvavllesDTRGKVRLPALHIAAkkDDVKAAT----------LLLDNDHNPD-VTSKSGFTPLH 210
Cdd:cd22194  215 -------ITSQ-------------DSRGNTVLHALVTVA--EDSKTQNdfvkrmydmiLLKSENKNLEtIRNNEGLTPLQ 272
                        170
                 ....*....|
gi 442630835 211 IASHYGNQNI 220
Cdd:cd22194  273 LAAKMGKAEI 282
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
383-523 6.06e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 63.43  E-value: 6.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 383 LKVVELLLRHGASISATTESGLTPLHVAAFMGCMNIVIYLLQHDASPDVPTVRGETPLHLAARANQTDIIRILLRNGAQV 462
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442630835 463 DARAREQQTPLHIASRLGNVDIVMLLLQHGAQVDATTKDMYTALHIAAKEGQDE-VKDLIAK 523
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEiVKLLLEA 142
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
386-522 6.36e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 65.27  E-value: 6.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 386 VELLLRHGASISATTESGLTPLHVAAFMGCMNIVIYLLQHDASPDVPTVRGETPLHLAARANQTDIIRILLRNgaqvdAR 465
Cdd:PLN03192 541 LEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHF-----AS 615
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 466 AREQQTP---LHIASRLGNVDIVMLLLQHGAQVDATTKDMYTALHIAAKEGQDEVKDLIA 522
Cdd:PLN03192 616 ISDPHAAgdlLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLI 675
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
263-444 6.46e-11

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 65.03  E-value: 6.46e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 263 NIEAKTRDGLTPLHCAARSGHEQVVDMLL--------ERGApisaktkNGLAPLHMAAQGEHVDAARILLyHRAPV---D 331
Cdd:cd22192    9 HLLQQKRISESPLLLAAKENDVQAIKKLLkcpscdlfQRGA-------LGETALHVAALYDNLEAAVVLM-EAAPElvnE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 332 EVTVD-YL--TALHVAAHCGHVRVAKLLLDRNAD-ANARALNGFTPLHI--------------ACKKNRlKVVELLLRHG 393
Cdd:cd22192   81 PMTSDlYQgeTALHIAVVNQNLNLVRELIARGADvVSPRATGTFFRPGPknliyygehplsfaACVGNE-EIVRLLIEHG 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442630835 394 ASISATTESGLTPLHVAAFMGCMNIV--IY--LLQHDASPD------VPTVRGETPLHLAA 444
Cdd:cd22192  160 ADIRAQDSLGNTVLHILVLQPNKTFAcqMYdlILSYDKEDDlqpldlVPNNQGLTPFKLAA 220
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
339-517 8.21e-11

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: 64.52  E-value: 8.21e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 339 TALHVAA---HCGHVRVAKLLLDRNAD-------ANARALN----GFTPLHIACKKNRLKVVELLLRHGASISATTESgl 404
Cdd:cd21882   28 TCLHKAAlnlNDGVNEAIMLLLEAAPDsgnpkelVNAPCTDefyqGQTALHIAIENRNLNLVRLLVENGADVSARATG-- 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 405 tplhvAAFMGCMNIVIYLlqhdaspdvptvrGETPLHLAARANQTDIIRILLRNGAQVdaRAREQQ-----TPLHIASRL 479
Cdd:cd21882  106 -----RFFRKSPGNLFYF-------------GELPLSLAACTNQEEIVRLLLENGAQP--AALEAQdslgnTVLHALVLQ 165
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 442630835 480 GN---------VDIVMLLLQHGAQVDATTK-------DMYTALHIAAKEGQDEV 517
Cdd:cd21882  166 ADntpensafvCQMYNLLLSYGAHLDPTQQleeipnhQGLTPLKLAAVEGKIVM 219
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
309-392 1.54e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 63.76  E-value: 1.54e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 309 HMAAQGEHVdAARILLYHRAPVDEVTVDYLTALHVAAHCGHVRVAKLLLDRNADANARALNGFTPLHIACKKNRLKVVEL 388
Cdd:PTZ00322  88 QLAASGDAV-GARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166

                 ....
gi 442630835 389 LLRH 392
Cdd:PTZ00322 167 LSRH 170
PHA02946 PHA02946
ankyin-like protein; Provisional
60-247 1.68e-10

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 63.15  E-value: 1.68e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  60 VSELLRRGAIVDSATKKGNTALHIASLAGQEEVVKLLLEHNASVNVQSQNGFTPLYMAAQENHDAVVR--LLLSNGA--N 135
Cdd:PHA02946  55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIERinLLVQYGAkiN 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 136 QSLaTEDGFTPLAVAM---QQGHDKVVAVLLESDTRGKVRLPALHIAAKKDDVKAATL--LLDNDHNPDVTSKSGFTPLH 210
Cdd:PHA02946 135 NSV-DEEGCGPLLACTdpsERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDNPKASTIswMMKLGISPSKPDHDGNTPLH 213
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 442630835 211 I--ASHYGNQNIANLLIqKGADVNYSAKHNISPLHVAAK 247
Cdd:PHA02946 214 IvcSKTVKNVDIINLLL-PSTDVNKQNKFGDSPLTLLIK 251
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
326-425 1.72e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 63.76  E-value: 1.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 326 HRAPVDEV---TVDYLTAL---HVAAHcGHVRVAKLLLDRNADANARALNGFTPLHIACKKNRLKVVELLLRHGASISAT 399
Cdd:PTZ00322  66 HNLTTEEVidpVVAHMLTVelcQLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLL 144
                         90       100
                 ....*....|....*....|....*.
gi 442630835 400 TESGLTPLHVAAFMGCMNIVIYLLQH 425
Cdd:PTZ00322 145 DKDGKTPLELAEENGFREVVQLLSRH 170
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
347-512 1.86e-10

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: 63.56  E-value: 1.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  347 CGHVRVAKLLLDRNADANARALN-------GFTPLHIACKKNRLK-VVELLLRHGASIsattESGLTPLHVAA---FMGC 415
Cdd:TIGR00870  22 LPAAERGDLASVYRDLEEPKKLNincpdrlGRSALFVAAIENENLeLTELLLNLSCRG----AVGDTLLHAISleyVDAV 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  416 MNIVIYLLQHDASPDVPTV----------RGETPLHLAARANQTDIIRILLRNGAQVDARA--------------REQQT 471
Cdd:TIGR00870  98 EAILLHLLAAFRKSGPLELandqytseftPGITALHLAAHRQNYEIVKLLLERGASVPARAcgdffvksqgvdsfYHGES 177
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 442630835  472 PLHIASRLGNVDIVMLLLQHGAQVDATTKDMYTALHIAAKE 512
Cdd:TIGR00870 178 PLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVME 218
Ank_4 pfam13637
Ankyrin repeats (many copies);
240-291 2.86e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.74  E-value: 2.86e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 442630835  240 SPLHVAAKWGKTNMVSLLLEKGGNIEAKTRDGLTPLHCAARSGHEQVVDMLL 291
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
11-154 5.68e-10

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: 61.95  E-value: 5.68e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  11 GNTSFLRAARAGNLERVLEHLKN-----NIDINTSNANGLNALHLASKDGHIHVVSELLRRGAIVDS--AT----KKGNT 79
Cdd:cd22192   51 GETALHVAALYDNLEAAVVLMEAapelvNEPMTSDLYQGETALHIAVVNQNLNLVRELIARGADVVSprATgtffRPGPK 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  80 AL-----HIASLA---GQEEVVKLLLEHNASVNVQSQNGFTPLYM-AAQENHDAVVR---LLLS---NGANQSLAT---E 141
Cdd:cd22192  131 NLiyygeHPLSFAacvGNEEIVRLLIEHGADIRAQDSLGNTVLHIlVLQPNKTFACQmydLILSydkEDDLQPLDLvpnN 210
                        170
                 ....*....|...
gi 442630835 142 DGFTPLAVAMQQG 154
Cdd:cd22192  211 QGLTPFKLAAKEG 223
Ank_4 pfam13637
Ankyrin repeats (many copies);
271-324 6.70e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.59  E-value: 6.70e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 442630835  271 GLTPLHCAARSGHEQVVDMLLERGAPISAKTKNGLAPLHMAAQGEHVDAARILL 324
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
10-140 6.87e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.16  E-value: 6.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  10 DGNTSFLRAARAGNLERVLEHLKNNIDINTSNANGLNALHLASKDGHIHVVSELLRRGAIVDSATKKGNTALHIASLAGQ 89
Cdd:PHA02875 101 DGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGD 180
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 442630835  90 EEVVKLLLEHNASVNVQSQNG-FTPLYMAAQENHDAVVRLLLSNGANQSLAT 140
Cdd:PHA02875 181 IAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNIMF 232
PHA02874 PHA02874
ankyrin repeat protein; Provisional
10-152 8.51e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 61.13  E-value: 8.51e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  10 DGNTSFLRAARAGNLERVLEHLKNNIDINTSNANGLNALHLASKDGHIHVVSELLRRGAIVDSATKKGNTALHIASLAGQ 89
Cdd:PHA02874 156 NGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR 235
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442630835  90 eEVVKLLLeHNASVNVQSQNGFTPLYMAAQENHDA-VVRLLLSNGANQSLATEDGFTPLAVAMQ 152
Cdd:PHA02874 236 -SAIELLI-NNASINDQDIDGSTPLHHAINPPCDIdIIDILLYHKADISIKDNKGENPIDTAFK 297
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
217-407 1.22e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 61.04  E-value: 1.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 217 NQNIANLLIQK-GADVNYSAKHNIspLHVAAKwGKTNMVSLLLEKGGNIEAKTRDGLTPLHCAARSGHEQVVDMLLERGA 295
Cdd:PLN03192 506 DLNVGDLLGDNgGEHDDPNMASNL--LTVAST-GNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHAC 582
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 296 PISAKTKNGLAPLHMAAQGEHVDAARIlLYHRAPVDE--VTVDYLTalhVAAHCGHVRVAKLLLDRNADANARALNGFTP 373
Cdd:PLN03192 583 NVHIRDANGNTALWNAISAKHHKIFRI-LYHFASISDphAAGDLLC---TAAKRNDLTAMKELLKQGLNVDSEDHQGATA 658
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 442630835 374 LHIACKKNRLKVVELLLRHGASI-SATTESGLTPL 407
Cdd:PLN03192 659 LQVAMAEDHVDMVRLLIMNGADVdKANTDDDFSPT 693
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
184-374 1.39e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 61.04  E-value: 1.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 184 DVKAATLLLDNDHNpDVTSKSGFTPLHIAShYGNQNIANLLIQKGADVNYSAKHNISPLHVAAKWGKTNMVSLLLEKGGN 263
Cdd:PLN03192 506 DLNVGDLLGDNGGE-HDDPNMASNLLTVAS-TGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACN 583
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 264 IEAKTRDGLTPLHCAARSGHEQVVDMLLERGAPISAKTKNGLapLHMAAQGEHVDAARILLYHRAPVDEVTVDYLTALHV 343
Cdd:PLN03192 584 VHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAGDL--LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQV 661
                        170       180       190
                 ....*....|....*....|....*....|..
gi 442630835 344 AAHCGHVRVAKLLLDRNADANARAL-NGFTPL 374
Cdd:PLN03192 662 AMAEDHVDMVRLLIMNGADVDKANTdDDFSPT 693
Ank_4 pfam13637
Ankyrin repeats (many copies);
337-390 2.41e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.05  E-value: 2.41e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 442630835  337 YLTALHVAAHCGHVRVAKLLLDRNADANARALNGFTPLHIACKKNRLKVVELLL 390
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
159-312 3.22e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 59.53  E-value: 3.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 159 VAVLLESDTRGKVRLPALHIAAKKDDVKAATLLLDNDHNPDVTSKSGFTPLHIASHyGNQNIANLLIQKGADVNYSAKHN 238
Cdd:PTZ00322  37 MAAIQEEIARIDTHLEALEATENKDATPDHNLTTEEVIDPVVAHMLTVELCQLAAS-GDAVGARILLTGGADPNCRDYDG 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 239 ISPLHVAAKWGKTNMVSLLLEKGGNIEAKTRDGLTPLHCAARSGHEQVVDMLLE----------RGAPISAKTKNGL--- 305
Cdd:PTZ00322 116 RTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRhsqchfelgaNAKPDSFTGKPPSled 195

                 ....*..
gi 442630835 306 APLHMAA 312
Cdd:PTZ00322 196 SPISSHH 202
PHA02859 PHA02859
ankyrin repeat protein; Provisional
207-343 3.26e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 57.14  E-value: 3.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 207 TPLH--IASHYGNQNIANLLIQKGADVNYSAKH-NISPLHVAAKWGKT---NMVSLLLEKGGNIEAKTRDGLTPLH---- 276
Cdd:PHA02859  53 TPIFscLEKDKVNVEILKFLIENGADVNFKTRDnNLSALHHYLSFNKNvepEILKILIDSGSSITEEDEDGKNLLHmymc 132
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442630835 277 -CAARSgheQVVDMLLERGAPISAKTKNGLAPLHmaaqgehvdaaRILLYHRapvDEVTVDYLTALHV 343
Cdd:PHA02859 133 nFNVRI---NVIKLLIDSGVSFLNKDFDNNNILY-----------SYILFHS---DKKIFDFLTSLGI 183
Ank_4 pfam13637
Ankyrin repeats (many copies);
304-357 4.79e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.28  E-value: 4.79e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 442630835  304 GLAPLHMAAQGEHVDAARILLYHRAPVDEVTVDYLTALHVAAHCGHVRVAKLLL 357
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
191-310 5.08e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 59.11  E-value: 5.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 191 LLDNDHNPDVTSKSGFTPLHIASHYGNQNIANLLIQKGADVNY-------------SAKHN-----------ISPLHV-- 244
Cdd:PLN03192 544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIrdangntalwnaiSAKHHkifrilyhfasISDPHAag 623
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442630835 245 -----AAKWGKTNMVSLLLEKGGNIEAKTRDGLTPLHCAARSGHEQVVDMLLERGAPI-SAKTKNGLAPLHM 310
Cdd:PLN03192 624 dllctAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVdKANTDDDFSPTEL 695
Ank_5 pfam13857
Ankyrin repeats (many copies);
355-410 5.18e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 52.35  E-value: 5.18e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 442630835  355 LLLDRNADANARALNGFTPLHIACKKNRLKVVELLLRHGASISATTESGLTPLHVA 410
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
372-423 5.66e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.28  E-value: 5.66e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 442630835  372 TPLHIACKKNRLKVVELLLRHGASISATTESGLTPLHVAAFMGCMNIVIYLL 423
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
418-510 2.38e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 56.21  E-value: 2.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 418 IVIYLLQHDASPDVPTVRGETPLHLAARANQTDIIRILLRNGAQVDARAREQQTPLHIASRLG-----NVDIVMLLLQHG 492
Cdd:PHA03100  17 NIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKynltdVKEIVKLLLEYG 96
                         90
                 ....*....|....*...
gi 442630835 493 AQVDATTKDMYTALHIAA 510
Cdd:PHA03100  97 ANVNAPDNNGITPLLYAI 114
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
243-334 3.60e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.06  E-value: 3.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 243 HVAAKwGKTNMVSLLLEKGGNIEAKTRDGLTPLHCAARSGHEQVVDMLLERGAPISAKTKNGLAPLHMAAQGEHVDAARI 322
Cdd:PTZ00322  88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166
                         90       100
                 ....*....|....*....|.
gi 442630835 323 LLYH---------RAPVDEVT 334
Cdd:PTZ00322 167 LSRHsqchfelgaNAKPDSFT 187
Ank_4 pfam13637
Ankyrin repeats (many copies);
77-130 4.38e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.58  E-value: 4.38e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 442630835   77 GNTALHIASLAGQEEVVKLLLEHNASVNVQSQNGFTPLYMAAQENHDAVVRLLL 130
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
370-527 8.27e-08

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: 55.20  E-value: 8.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 370 GFTPLHIACKKNRLKVVELLLRHGASISATTeSGltplhvaafmgcmnivIYLLQHDASPDVptVRGETPLHLAARANQT 449
Cdd:cd22196   94 GQTALHIAIERRNMHLVELLVQNGADVHARA-SG----------------EFFKKKKGGPGF--YFGELPLSLAACTNQL 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 450 DIIRILLRN---GAQVDARAREQQTPLH----IA-SRLGNVDIVML----LLQHGAQV-------DATTKDMYTALHIAA 510
Cdd:cd22196  155 DIVKFLLENphsPADISARDSMGNTVLHalveVAdNTPENTKFVTKmyneILILGAKIrpllkleEITNKKGLTPLKLAA 234
                        170
                 ....*....|....*...
gi 442630835 511 KEGQDEV-KDLIAKKITD 527
Cdd:cd22196  235 KTGKIGIfAYILGREIKE 252
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
339-478 1.06e-07

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: 54.50  E-value: 1.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 339 TALHVAAHCGHVRVAKLLLDRNADANARALNGF-------------TPLHIACKKNRLKVVELLLRHG---ASISATTES 402
Cdd:cd21882   75 TALHIAIENRNLNLVRLLVENGADVSARATGRFfrkspgnlfyfgeLPLSLAACTNQEEIVRLLLENGaqpAALEAQDSL 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 403 GLTPLHV-------AAFMGCMNIVIY--LLQHDASPD-------VPTVRGETPLHLAARANQTDIIRILLRngaqvdara 466
Cdd:cd21882  155 GNTVLHAlvlqadnTPENSAFVCQMYnlLLSYGAHLDptqqleeIPNHQGLTPLKLAAVEGKIVMFQHILQ--------- 225
                        170
                 ....*....|..
gi 442630835 467 REQQTPLHIASR 478
Cdd:cd21882  226 REFSGPYQPLSR 237
PHA02798 PHA02798
ankyrin-like protein; Provisional
250-529 1.14e-07

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 54.46  E-value: 1.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 250 KTNMVSLLLEKGGNIEAKTRDGLTPLhCAARSGHEQ------VVDMLLERGAPISAKTKNGLAPLHMAAQGEHVDAARIL 323
Cdd:PHA02798  50 STDIVKLFINLGANVNGLDNEYSTPL-CTILSNIKDykhmldIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEIL 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 324 LY---HRAPVDEVTVDYLTALHVAAHCGH---VRVAKLLLDRNADANARA-LNGFTPLHIACKKN----RLKVVELLLRH 392
Cdd:PHA02798 129 LFmieNGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINTHNnKEKYDTLHCYFKYNidriDADILKLFVDN 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 393 GASISATTESgltplHVAAFMGCMNIVIYLLQHDASP---------DVPTVR--GETPLHLAARANQTDIIRILLRNGAQ 461
Cdd:PHA02798 209 GFIINKENKS-----HKKKFMEYLNSLLYDNKRFKKNildfifsyiDINQVDelGFNPLYYSVSHNNRKIFEYLLQLGGD 283
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442630835 462 VDARAREQQTPLHIASRLGNVDIVMLLLQHGAQVDATTKDMYT-ALHIAAKEGQ--DEVKDLIAKKITDHI 529
Cdd:PHA02798 284 INIITELGNTCLFTAFENESKFIFNSILNKKPNKNTISYTYYKlRKHILNVEGDfiNQLEFDIIKKFIAYV 354
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
437-523 1.30e-07

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: 54.25  E-value: 1.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 437 ETPLHLAARANQTDIIRILLR-NGAQVDARAREQQTPLHIASRLGNVDIVMLLLQHGAQV--DATTKDMY---TALHIA- 509
Cdd:cd22192   18 ESPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELvnEPMTSDLYqgeTALHIAv 97
                         90
                 ....*....|....
gi 442630835 510 AKEGQDEVKDLIAK 523
Cdd:cd22192   98 VNQNLNLVRELIAR 111
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
93-163 1.47e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.13  E-value: 1.47e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442630835  93 VKLLLEHNASVNVQSQNGFTPLYMAAQENHDAVVRLLLSNGANQSLATEDGFTPLAVAMQQGHDKVVAVLL 163
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
Ank_4 pfam13637
Ankyrin repeats (many copies);
44-97 2.16e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.65  E-value: 2.16e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 442630835   44 GLNALHLASKDGHIHVVSELLRRGAIVDSATKKGNTALHIASLAGQEEVVKLLL 97
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
410-534 2.31e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 53.07  E-value: 2.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 410 AAFMGCMNIVIYLLQHDASPDVPTVRGETPLHLAARANQTDIIRILLRNGAQVDARAREQQTPLHIASRLGNVDIVMLLL 489
Cdd:PHA02875   9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 442630835 490 QHGAQV-DATTKDMYTALHIAAK-EGQDEVKDLIAKKI------TDHIDTVYL 534
Cdd:PHA02875  89 DLGKFAdDVFYKDGMTPLHLATIlKKLDIMKLLIARGAdpdipnTDKFSPLHL 141
Ank_4 pfam13637
Ankyrin repeats (many copies);
438-489 2.39e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.65  E-value: 2.39e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 442630835  438 TPLHLAARANQTDIIRILLRNGAQVDARAREQQTPLHIASRLGNVDIVMLLL 489
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
370-527 2.51e-07

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: 53.32  E-value: 2.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 370 GFTPLHIACKKNRLKVVELLLRHGASISATTESGLtplhvaaFMGCMNIVIYLlqhdaspdvptvrGETPLHLAARANQT 449
Cdd:cd22197   94 GHSALHIAIEKRSLQCVKLLVENGADVHARACGRF-------FQKKQGTCFYF-------------GELPLSLAACTKQW 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 450 DIIRILLRNGAQVdARAREQ----QTPLH----IASRLG-NVDIVML----LLQHGAQVDATTK-------DMYTALHIA 509
Cdd:cd22197  154 DVVNYLLENPHQP-ASLQAQdslgNTVLHalvmIADNSPeNSALVIKmydgLLQAGARLCPTVQleeisnhEGLTPLKLA 232
                        170
                 ....*....|....*....
gi 442630835 510 AKEGQDEV-KDLIAKKITD 527
Cdd:cd22197  233 AKEGKIEIfRHILQREFSG 251
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
11-248 3.76e-07

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 53.16  E-value: 3.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835   11 GNTSFLRAARAGNLERVLEHLKNNidiNTSNANGLNALHLASKdGHIHVVSELLR------RGA-----IVDSATK---K 76
Cdd:TIGR00870  52 GRSALFVAAIENENLELTELLLNL---SCRGAVGDTLLHAISL-EYVDAVEAILLhllaafRKSgplelANDQYTSeftP 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835   77 GNTALHIASLAGQEEVVKLLLEHNASVNV----------QSQNGF----TPLYMAAQENHDAVVRLLLSNGANQSLATED 142
Cdd:TIGR00870 128 GITALHLAAHRQNYEIVKLLLERGASVPAracgdffvksQGVDSFyhgeSPLNAAACLGSPSIVALLSEDPADILTADSL 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  143 GFTPLAVAMQQGHDKVVAVLLESdtrgKVRLPALHIAAKKDDVKAATLLLDNDhnpdvtsksGFTPLHIASHYGNQNIAN 222
Cdd:TIGR00870 208 GNTLLHLLVMENEFKAEYEELSC----QMYNFALSLLDKLRDSKELEVILNHQ---------GLTPLKLAAKEGRIVLFR 274
                         250       260       270
                  ....*....|....*....|....*....|
gi 442630835  223 LLIQkgadVNYSAK----HNISPLHVAAKW 248
Cdd:TIGR00870 275 LKLA----IKYKQKkfvaWPNGQQLLSLYW 300
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
422-491 5.77e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.21  E-value: 5.77e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 422 LLQHDASPDVPTVRGETPLHLAARANQTDIIRILLRNGAQVDARAREQQTPLHIASRLGNVDIVMLLLQH 491
Cdd:PTZ00322 101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
Ank_4 pfam13637
Ankyrin repeats (many copies);
403-456 5.88e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.50  E-value: 5.88e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 442630835  403 GLTPLHVAAFMGCMNIVIYLLQHDASPDVPTVRGETPLHLAARANQTDIIRILL 456
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
172-225 5.94e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.50  E-value: 5.94e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 442630835  172 RLPALHIAAKKDDVKAATLLLDNDHNPDVTSKSGFTPLHIASHYGNQNIANLLI 225
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
63-131 6.40e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.21  E-value: 6.40e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442630835  63 LLRRGAIVDSATKKGNTALHIASLAGQEEVVKLLLEHNASVNVQSQNGFTPLYMAAQENHDAVVRLLLS 131
Cdd:PTZ00322 101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
PHA02876 PHA02876
ankyrin repeat protein; Provisional
20-163 9.77e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 51.60  E-value: 9.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  20 RAGNLER----VLEHLKNNIDINTSNANGLNALHLASKDGHIHVVSELLRRGAIVDSATKKGNTALHIAsLAGQEEV--V 93
Cdd:PHA02876 347 QASTLDRnkdiVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFA-LCGTNPYmsV 425
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442630835  94 KLLLEHNASVNVQSQNGFTPLYMAAQEN-HDAVVRLLLSNGANQSLATEDGFTPLAVAMqqGHDKVVAVLL 163
Cdd:PHA02876 426 KTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILL 494
PHA02989 PHA02989
ankyrin repeat protein; Provisional
31-293 1.27e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 50.90  E-value: 1.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  31 LKNNIDINTS-NANGLNALHLASKDGHIHVVSELLRRGAIVDSatkKGNTALHIASLAGQEEV--------VKLLLEHNA 101
Cdd:PHA02989  23 LRTGFDVNEEyRGNSILLLYLKRKDVKIKIVKLLIDNGADVNY---KGYIETPLCAVLRNREItsnkikkiVKLLLKFGA 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 102 SVNVQSQNGFTP----LYMAAQENHDaVVRLLLSNGAN-QSLATEDGFTPLAVAMQQGHDK--VVAVLLES-----DTRG 169
Cdd:PHA02989 100 DINLKTFNGVSPivcfIYNSNINNCD-MLRFLLSKGINvNDVKNSRGYNLLHMYLESFSVKkdVIKILLSFgvnlfEKTS 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 170 KVRLPALHIAAKKD----DVKAATLLLDND---HNPDVTSKS---GFTPLHIASHYGNQNIANLlIQKGADVNYSAKHNI 239
Cdd:PHA02989 179 LYGLTPMNIYLRNDidviSIKVIKYLIKKGvniETNNNGSESvleSFLDNNKILSKKEFKVLNF-ILKYIKINKKDKKGF 257
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 442630835 240 SPLHVAAKWGKTNMVSLLLEKGGNIEAKTRDGLTPLHCAARSGHEQVVDMLLER 293
Cdd:PHA02989 258 NPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLNRILQL 311
PHA02878 PHA02878
ankyrin repeat protein; Provisional
341-517 1.66e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 50.65  E-value: 1.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 341 LHVAAHCGHVRVAKLLLDRNADANARALNGFTPLHIACKK-NRLKVVELllrhgasISATTESGLTPLHVAAFMGCMNIV 419
Cdd:PHA02878  41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEpNKLGMKEM-------IRSINKCSVFYTLVAIKDAFNNRN 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 420 IYLLQ------HDASPDVPTVRGETPLHlaARANQTDIIRILLRNGAQVDARAREQ-QTPLHIASRLGNVDIVMLLLQHG 492
Cdd:PHA02878 114 VEIFKiiltnrYKNIQTIDLVYIDKKSK--DDIIEAEITKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYG 191
                        170       180
                 ....*....|....*....|....*
gi 442630835 493 AQVDATTKDMYTALHIAAKEGQDEV 517
Cdd:PHA02878 192 ANVNIPDKTNNSPLHHAVKHYNKPI 216
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
386-457 1.85e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.67  E-value: 1.85e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442630835 386 VELLLRHGASISATTESGLTPLHVAAFMGCMNIVIYLLQHDASPDVPTVRGETPLHLAARANQTDIIRILLR 457
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
360-527 1.88e-06

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: 50.56  E-value: 1.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 360 NADANARALNGFTPLHIACKKNRLKVVELLLRHGASISATTESgltplhvaafmgcmnivIYLLQHDASPDVptVRGETP 439
Cdd:cd22193   66 NAEYTDEYYEGQTALHIAIERRQGDIVALLVENGADVHAHAKG-----------------RFFQPKYQGEGF--YFGELP 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 440 LHLAARANQTDIIRILLRNGAQ-VDARAREQ--QTPLH----IASRL-GNVDIVM----LLLQHGAQVDATTK------- 500
Cdd:cd22193  127 LSLAACTNQPDIVQYLLENEHQpADIEAQDSrgNTVLHalvtVADNTkENTKFVTrmydMILIRGAKLCPTVEleeirnn 206
                        170       180
                 ....*....|....*....|....*...
gi 442630835 501 DMYTALHIAAKEGQDEV-KDLIAKKITD 527
Cdd:cd22193  207 DGLTPLQLAAKMGKIEIlKYILQREIKE 234
Ank_4 pfam13637
Ankyrin repeats (many copies);
471-514 2.15e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.96  E-value: 2.15e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 442630835  471 TPLHIASRLGNVDIVMLLLQHGAQVDATTKDMYTALHIAAKEGQ 514
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGN 46
PHA02946 PHA02946
ankyin-like protein; Provisional
191-516 2.37e-06

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 50.05  E-value: 2.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 191 LLDNDHNPDVTSKSGFTPLHIASHYGNQNIANLLIQKGADVNYSAKHNISPLHVAAKWGK--TNMVSLLLEKGGNIEAKT 268
Cdd:PHA02946  58 LLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKINNSV 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 269 -RDGLTPLhCAARSGHEQVVDMLLERGAPISAKTKNGLAPLHMAAQGEHVDAARILLYHRAPVDEVTVDY--LTALHV-- 343
Cdd:PHA02946 138 dEEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDNPKASTISWMMKLGISPSKPDHdgNTPLHIvc 216
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 344 AAHCGHVRVAKLLLDrNADANARALNGFTPLHIACKK-NRLKVVELLLRHGASISATT---------------------E 401
Cdd:PHA02946 217 SKTVKNVDIINLLLP-STDVNKQNKFGDSPLTLLIKTlSPAHLINKLLSTSNVITDQTvnicifydrddvleiindkgkQ 295
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 402 SGLTPLHVAAFMGCMNIVIYLLQHDaspdvptVRGETPLHLAARANQTDIIRILLRNGAQVDArAREQQTPLHIASRLGN 481
Cdd:PHA02946 296 YDSTDFKMAVEVGSIRCVKYLLDND-------IICEDAMYYAVLSEYETMVDYLLFNHFSVDS-VVNGHTCMSECVRLNN 367
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 442630835 482 VDIVMLLLQHgaqvDATTKDMYTALHIAAKEGQDE 516
Cdd:PHA02946 368 PVILSKLMLH----NPTSETMYLTMKAIEKDKLDK 398
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
22-257 2.69e-06

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: 50.26  E-value: 2.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  22 GNLERVLEHLKNniDINTSNANGLNALHLAS---KDGHIHVVSELLRRGAIVDSATK-----------KGNTALHIASLA 87
Cdd:cd21882    6 GLLECLRWYLTD--SAYQRGATGKTCLHKAAlnlNDGVNEAIMLLLEAAPDSGNPKElvnapctdefyQGQTALHIAIEN 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  88 GQEEVVKLLLEHNASVNVQS---------QNGF----TPLYMAAQENHDAVVRLLLSNGANqslatedgftplavamqqg 154
Cdd:cd21882   84 RNLNLVRLLVENGADVSARAtgrffrkspGNLFyfgeLPLSLAACTNQEEIVRLLLENGAQ------------------- 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 155 hdkvVAVLLESDTRGKVRLPALHIAAKK--DDVKAAT----LLLDNDHNPD-------VTSKSGFTPLHIASHYGNQNIA 221
Cdd:cd21882  145 ----PAALEAQDSLGNTVLHALVLQADNtpENSAFVCqmynLLLSYGAHLDptqqleeIPNHQGLTPLKLAAVEGKIVMF 220
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 442630835 222 NLLIQKGADVNY---SAKHN---ISPLHVAA-------KWGKTNMVSLL 257
Cdd:cd21882  221 QHILQREFSGPYqplSRKFTewtYGPVTSSLydlseidSWEKNSVLELI 269
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
26-99 3.69e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.90  E-value: 3.69e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442630835  26 RVLehLKNNIDINTSNANGLNALHLASKDGHIHVVSELLRRGAIVDSATKKGNTALHIASLAGQEEVVKLLLEH 99
Cdd:PTZ00322  99 RIL--LTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
91-463 4.72e-06

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 49.53  E-value: 4.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  91 EVVKLLLEHNASVNVQSQNGFTPL--YMAAQENHDAVVRLLLSNGANQSLATEDGFTPLAVAMQQG---HDKVVAVLLES 165
Cdd:PHA02716 193 DILEWLCNNGVNVNLQNNHLITPLhtYLITGNVCASVIKKIIELGGDMDMKCVNGMSPIMTYIINIdniNPEITNIYIES 272
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 166 DTRGKVR-LPA-LHI---AAKKDDVKAATLLLDNDHNPDVTSKSGFTPLH--IASHYGNQNIANLLIQKGADVNYSAKHN 238
Cdd:PHA02716 273 LDGNKVKnIPMiLHSyitLARNIDISVVYSFLQPGVKLHYKDSAGRTCLHqyILRHNISTDIIKLLHEYGNDLNEPDNIG 352
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 239 ISPLH--------VAAKWGKTN------MVSLLLEKGGNIEAKTRDGLTPLH---CAARS-GHEQVVDMLlergapISAK 300
Cdd:PHA02716 353 NTVLHtylsmlsvVNILDPETDndirldVIQCLISLGADITAVNCLGYTPLTsyiCTAQNyMYYDIIDCL------ISDK 426
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 301 TKNGLAPLHMAAQGEHVDAARILLYH-----RAPVDEVTVDY----LTALHVAAHCGHVrvakllldRNADANARALNGF 371
Cdd:PHA02716 427 VLNMVKHRILQDLLIRVDDTPCIIHHiiakyNIPTDLYTDEYepydSTKIHDVYHCAII--------ERYNNAVCETSGM 498
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 372 TPLHIA-CKKNRLKVVelllrhgasisattesgltplhvaafmgcMNIVIYLLQHDASPDVPTVRGETPLHLAARAN--- 447
Cdd:PHA02716 499 TPLHVSiISHTNANIV-----------------------------MDSFVYLLSIQYNINIPTKNGVTPLMLTMRNNrls 549
                        410
                 ....*....|....*...
gi 442630835 448 --QTDIIRILLRNGAQVD 463
Cdd:PHA02716 550 ghQWYIVKNILDKRPNVD 567
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
339-456 4.92e-06

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: 49.37  E-value: 4.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 339 TALHVAAHCGHVRVAKLLLDRNADANARA----------LNGF----TPLHIACKKNRLKVVELLLRHGASISATTES-G 403
Cdd:cd22194  143 TALNIAIERRQGDIVKLLIAKGADVNAHAkgvffnpkykHEGFyfgeTPLALAACTNQPEIVQLLMEKESTDITSQDSrG 222
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442630835 404 LTPLH----VA-------AFMGCMNIVIYLLQHDASPD-VPTVRGETPLHLAARANQTDIIRILL 456
Cdd:cd22194  223 NTVLHalvtVAedsktqnDFVKRMYDMILLKSENKNLEtIRNNEGLTPLQLAAKMGKAEILKYIL 287
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
10-114 5.16e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 49.48  E-value: 5.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  10 DGNTSFLRAARAGNLE--RVLEHLKNNIDINTSNanglNALHLASKDGHIHVVSELLRRGAIVDSATKKGNTALHIASLA 87
Cdd:PLN03192 590 NGNTALWNAISAKHHKifRILYHFASISDPHAAG----DLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAE 665
                         90       100
                 ....*....|....*....|....*...
gi 442630835  88 GQEEVVKLLLEHNASVN-VQSQNGFTPL 114
Cdd:PLN03192 666 DHVDMVRLLIMNGADVDkANTDDDFSPT 693
Ank_5 pfam13857
Ankyrin repeats (many copies);
422-476 5.68e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.87  E-value: 5.68e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 442630835  422 LLQHD-ASPDVPTVRGETPLHLAARANQTDIIRILLRNGAQVDARAREQQTPLHIA 476
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
191-245 5.85e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.87  E-value: 5.85e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 442630835  191 LLDNDH-NPDVTSKSGFTPLHIASHYGNQNIANLLIQKGADVNYSAKHNISPLHVA 245
Cdd:pfam13857   1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
207-258 6.91e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.42  E-value: 6.91e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 442630835  207 TPLHIASHYGNQNIANLLIQKGADVNYSAKHNISPLHVAAKWGKTNMVSLLL 258
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02884 PHA02884
ankyrin repeat protein; Provisional
207-280 7.71e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 48.06  E-value: 7.71e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442630835 207 TPLHIASHYGNQNIANLLIQKGADVN-YSAKHNISPLHVAAKWGKTNMVSLLLEKGGNIEAKTRDGLTPLHCAAR 280
Cdd:PHA02884  72 NPLIYAIDCDNDDAAKLLIRYGADVNrYAEEAKITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELALM 146
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
357-517 1.11e-05

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 48.22  E-value: 1.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 357 LDR--NADANARALNGFTPLHIACKKNRLKVVELLLRHGASISATTESG-LTPLHvaafmgcmniviyllQHDAspdvpT 433
Cdd:cd22194  126 LDRfiNAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVfFNPKY---------------KHEG-----F 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 434 VRGETPLHLAARANQTDIIRILLRN----GAQVDARAreqQTPLH----IASRL-GNVDIV-----MLLLQHGAQ-VDAT 498
Cdd:cd22194  186 YFGETPLALAACTNQPEIVQLLMEKestdITSQDSRG---NTVLHalvtVAEDSkTQNDFVkrmydMILLKSENKnLETI 262
                        170       180
                 ....*....|....*....|
gi 442630835 499 T-KDMYTALHIAAKEGQDEV 517
Cdd:cd22194  263 RnNEGLTPLQLAAKMGKAEI 282
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
369-398 1.21e-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: 42.19  E-value: 1.21e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 442630835   369 NGFTPLHIACKKNRLKVVELLLRHGASISA 398
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
389-443 1.96e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 1.96e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 442630835  389 LLRHG-ASISATTESGLTPLHVAAFMGCMNIVIYLLQHDASPDVPTVRGETPLHLA 443
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
76-227 2.06e-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: 47.49  E-value: 2.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  76 KGNTALHIASLAGQEEVVKLLLEHNASVN----------VQSQNGF----TPLYMAAQENHDAVVRLLLSNganqslate 141
Cdd:cd22196   93 KGQTALHIAIERRNMHLVELLVQNGADVHarasgeffkkKKGGPGFyfgeLPLSLAACTNQLDIVKFLLEN--------- 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 142 dgftPLAVAmqqghdKVVAVllesDTRGKVRLPALHIAA--KKDDVKAAT------LLLDNDHNP-----DVTSKSGFTP 208
Cdd:cd22196  164 ----PHSPA------DISAR----DSMGNTVLHALVEVAdnTPENTKFVTkmyneiLILGAKIRPllkleEITNKKGLTP 229
                        170
                 ....*....|....*....
gi 442630835 209 LHIASHYGNQNIANLLIQK 227
Cdd:cd22196  230 LKLAAKTGKIGIFAYILGR 248
Ank_5 pfam13857
Ankyrin repeats (many copies);
339-377 2.29e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 2.29e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 442630835  339 TALHVAAHCGHVRVAKLLLDRNADANARALNGFTPLHIA 377
Cdd:pfam13857  18 TPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02884 PHA02884
ankyrin repeat protein; Provisional
417-511 2.57e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 46.13  E-value: 2.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 417 NIVIYLLQHDASPDVPTVRGE----TPLHLAARANQTDIIRILLRNGAQVDARAREQQ-TPLHIASRLGNVDIVMLLLQH 491
Cdd:PHA02884  47 DIIDAILKLGADPEAPFPLSEnsktNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLHGCLKCLEILLSY 126
                         90       100
                 ....*....|....*....|
gi 442630835 492 GAQVDATTKDMYTALHIAAK 511
Cdd:PHA02884 127 GADINIQTNDMVTPIELALM 146
Ank_5 pfam13857
Ankyrin repeats (many copies);
455-509 2.60e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 2.60e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 442630835  455 LLRNG-AQVDARAREQQTPLHIASRLGNVDIVMLLLQHGAQVDATTKDMYTALHIA 509
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
270-302 2.96e-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: 41.12  E-value: 2.96e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 442630835  270 DGLTPLHCAA-RSGHEQVVDMLLERGAPISAKTK 302
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
339-457 3.40e-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: 3.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 339 TALHVAAHCGHVRVAKLLLDRNADANARAL----------NGF----TPLHIACKKNRLKVVELLLRH---GASISATTE 401
Cdd:cd22196   96 TALHIAIERRNMHLVELLVQNGADVHARASgeffkkkkggPGFyfgeLPLSLAACTNQLDIVKFLLENphsPADISARDS 175
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442630835 402 SGLTPLH----VA-------AFMGCMNIVIYLLQHDASP-----DVPTVRGETPLHLAARANQTDIIRILLR 457
Cdd:cd22196  176 MGNTVLHalveVAdntpentKFVTKMYNEILILGAKIRPllkleEITNKKGLTPLKLAAKTGKIGIFAYILG 247
PHA02798 PHA02798
ankyrin-like protein; Provisional
31-264 5.02e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 45.98  E-value: 5.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  31 LKNNIDINTSNANGLNALHLASKDGHIH---VVSELLRRGAIVDSATKKGNTALHIASLAG---QEEVVKLLLEHNASVN 104
Cdd:PHA02798  96 IENGADINKKNSDGETPLYCLLSNGYINnleILLFMIENGADTTLLDKDGFTMLQVYLQSNhhiDIEIIKLLLEKGVDIN 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 105 VQS-QNGFTPLYMAAQENHDA----VVRLLLSNGAnqSLATEDGFTPlavamQQGHDKVVAVLLESDtrgKVRLPALHIA 179
Cdd:PHA02798 176 THNnKEKYDTLHCYFKYNIDRidadILKLFVDNGF--IINKENKSHK-----KKFMEYLNSLLYDNK---RFKKNILDFI 245
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 180 AKKDDVkaatllldNDHNpdvtsKSGFTPLHIASHYGNQNIANLLIQKGADVNYSAKHNISPLHVAAKWGKTNMVSLLLE 259
Cdd:PHA02798 246 FSYIDI--------NQVD-----ELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILN 312

                 ....*
gi 442630835 260 KGGNI 264
Cdd:PHA02798 313 KKPNK 317
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
369-401 5.66e-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: 5.66e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 442630835  369 NGFTPLHIACKK-NRLKVVELLLRHGASISATTE 401
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
369-398 6.70e-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: 39.93  E-value: 6.70e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 442630835  369 NGFTPLHIACKKNRLKVVELLLRHGASISA 398
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
11-64 7.23e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.72  E-value: 7.23e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 442630835   11 GNTSFLRAARAGNLERVLEHLKNNIDINTSNANGLNALHLASKDGHIHVVSELL 64
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
224-278 8.22e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.41  E-value: 8.22e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 442630835  224 LIQKG-ADVNYSAKHNISPLHVAAKWGKTNMVSLLLEKGGNIEAKTRDGLTPLHCA 278
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
76-105 9.43e-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: 9.43e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 442630835    76 KGNTALHIASLAGQEEVVKLLLEHNASVNV 105
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02946 PHA02946
ankyin-like protein; Provisional
359-469 9.60e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 45.04  E-value: 9.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 359 RNADANARALNGFTP------LHIACKKNRL--KVVELLLRHGASISATTESGLTPLHVAAFMGCMNIVIYLLQHDASPD 430
Cdd:PHA02946  20 KNLDVFRNMLQAIEPsgnyhiLHAYCGIKGLdeRFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPN 99
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 442630835 431 VPTVRGETPLHLAARANQTDIIRI--LLRNGAQVDARAREQ 469
Cdd:PHA02946 100 ACDKQHKTPLYYLSGTDDEVIERInlLVQYGAKINNSVDEE 140
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
339-457 9.77e-05

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: 45.23  E-value: 9.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 339 TALHVAAHCGHVRVAKLLLDRNADANARALNGF-------------TPLHIACKKNRLKVVELLLRHG---ASISATTES 402
Cdd:cd22197   96 SALHIAIEKRSLQCVKLLVENGADVHARACGRFfqkkqgtcfyfgeLPLSLAACTKQWDVVNYLLENPhqpASLQAQDSL 175
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442630835 403 GLTPLHVAAFMG-----CMNIVIY----LLQHDASPDvPTVR--------GETPLHLAARANQTDIIRILLR 457
Cdd:cd22197  176 GNTVLHALVMIAdnspeNSALVIKmydgLLQAGARLC-PTVQleeisnheGLTPLKLAAKEGKIEIFRHILQ 246
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
205-313 1.03e-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: 45.17  E-value: 1.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 205 GFTPLHIASHYGNQNIANLLIQKGADVNYSAKHNI--------------SPLHVAAKWGKTNMVSLLLE---KGGNIEAK 267
Cdd:cd22193   76 GQTALHIAIERRQGDIVALLVENGADVHAHAKGRFfqpkyqgegfyfgeLPLSLAACTNQPDIVQYLLEnehQPADIEAQ 155
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442630835 268 TRDGLTPLHC---AARSGHEQ------VVDMLLERGAPISAKTK-------NGLAPLHMAAQ 313
Cdd:cd22193  156 DSRGNTVLHAlvtVADNTKENtkfvtrMYDMILIRGAKLCPTVEleeirnnDGLTPLQLAAK 217
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
339-457 1.05e-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: 45.17  E-value: 1.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 339 TALHVAAHCGHVRVAKLLLDRNADANARALNGF--------------TPLHIACKKNRLKVVELLLRHG---ASISATTE 401
Cdd:cd22193   78 TALHIAIERRQGDIVALLVENGADVHAHAKGRFfqpkyqgegfyfgeLPLSLAACTNQPDIVQYLLENEhqpADIEAQDS 157
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442630835 402 SGLTPLH----VA-------AFMGCMNIVIYLLQHDASPDVP--TVR---GETPLHLAARANQTDIIRILLR 457
Cdd:cd22193  158 RGNTVLHalvtVAdntkentKFVTRMYDMILIRGAKLCPTVEleEIRnndGLTPLQLAAKMGKIEILKYILQ 229
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
205-233 1.11e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.49  E-value: 1.11e-04
                           10        20
                   ....*....|....*....|....*....
gi 442630835   205 GFTPLHIASHYGNQNIANLLIQKGADVNY 233
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
270-299 1.28e-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: 39.16  E-value: 1.28e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 442630835  270 DGLTPLHCAARSGHEQVVDMLLERGAPISA 299
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
256-311 1.33e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.02  E-value: 1.33e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 442630835  256 LLLEKGGNIEAKTRDGLTPLHCAARSGHEQVVDMLLERGAPISAKTKNGLAPLHMA 311
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
205-313 1.52e-04

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 44.75  E-value: 1.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 205 GFTPLHIASHYGNQNIANLLIQKGADVNYSAKHNI--------------SPLHVAAKWGKTNMVSLLLEKGG-NIEAKTR 269
Cdd:cd22194  141 GQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVFfnpkykhegfyfgeTPLALAACTNQPEIVQLLMEKEStDITSQDS 220
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 442630835 270 DGLTPLHC---AARSGHEQ------VVDMLLERGAPISAKT---KNGLAPLHMAAQ 313
Cdd:cd22194  221 RGNTVLHAlvtVAEDSKTQndfvkrMYDMILLKSENKNLETirnNEGLTPLQLAAK 276
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
76-106 1.60e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.19  E-value: 1.60e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 442630835   76 KGNTALHIASL-AGQEEVVKLLLEHNASVNVQ 106
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNAR 32
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
470-500 1.64e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.81  E-value: 1.64e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 442630835  470 QTPLHIAS-RLGNVDIVMLLLQHGAQVDATTK 500
Cdd:pfam00023   3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
270-299 2.35e-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: 38.34  E-value: 2.35e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 442630835   270 DGLTPLHCAARSGHEQVVDMLLERGAPISA 299
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
205-232 3.01e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.42  E-value: 3.01e-04
                          10        20
                  ....*....|....*....|....*....
gi 442630835  205 GFTPLHIAS-HYGNQNIANLLIQKGADVN 232
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVN 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
435-465 3.39e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.04  E-value: 3.39e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 442630835  435 RGETPLHLAA-RANQTDIIRILLRNGAQVDAR 465
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNAR 32
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
18-103 3.41e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 43.70  E-value: 3.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  18 AARAGNLERVLEHLKNNIDINTSNANGLNALHLASKDGHIHVVSELLRRGAIVDSAtkkgNTALHIASLAGQEEVVKLLL 97
Cdd:PLN03192 629 AAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKA----NTDDDFSPTELRELLQKREL 704

                 ....*.
gi 442630835  98 EHNASV 103
Cdd:PLN03192 705 GHSITI 710
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
44-181 3.55e-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: 43.25  E-value: 3.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  44 GLNALHLASKDGHIHVVSELLRRGAIVDSATKK--------------GNTALHIASLAGQEEVVKLLLEH---NASVNVQ 106
Cdd:cd22193   76 GQTALHIAIERRQGDIVALLVENGADVHAHAKGrffqpkyqgegfyfGELPLSLAACTNQPDIVQYLLENehqPADIEAQ 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 107 SQNGFTPLY---MAAQ---ENHDAVVR---LLLSNGAN-------QSLATEDGFTPLAVAMQQGHDKVVAVLLESDTRGK 170
Cdd:cd22193  156 DSRGNTVLHalvTVADntkENTKFVTRmydMILIRGAKlcptvelEEIRNNDGLTPLQLAAKMGKIEILKYILQREIKEP 235
                        170
                 ....*....|.
gi 442630835 171 vrlPALHIAAK 181
Cdd:cd22193  236 ---ELRHLSRK 243
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
435-507 3.66e-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: 3.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 435 RGETPLHLAARANQTDIIRILLRNGAQVDARAREQ--------------QTPLHIASRLGNVDIVMLLLQH---GAQVDA 497
Cdd:cd22196   93 KGQTALHIAIERRNMHLVELLVQNGADVHARASGEffkkkkggpgfyfgELPLSLAACTNQLDIVKFLLENphsPADISA 172
                         90
                 ....*....|
gi 442630835 498 TTKDMYTALH 507
Cdd:cd22196  173 RDSMGNTVLH 182
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
76-227 3.77e-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: 43.25  E-value: 3.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  76 KGNTALHIASLAGQEEVVKLLLEHNASVNVQSQNGF--------------TPLYMAAQENHDAVVRLLLSNganqslate 141
Cdd:cd22193   75 EGQTALHIAIERRQGDIVALLVENGADVHAHAKGRFfqpkyqgegfyfgeLPLSLAACTNQPDIVQYLLEN--------- 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 142 dgftplavamqqGHDKvvAVLLESDTRGKVRLPALHIAAK--KDDVKAAT------LLLDNDHNPDV-----TSKSGFTP 208
Cdd:cd22193  146 ------------EHQP--ADIEAQDSRGNTVLHALVTVADntKENTKFVTrmydmiLIRGAKLCPTVeleeiRNNDGLTP 211
                        170
                 ....*....|....*....
gi 442630835 209 LHIASHYGNQNIANLLIQK 227
Cdd:cd22193  212 LQLAAKMGKIEILKYILQR 230
PHA02946 PHA02946
ankyin-like protein; Provisional
213-442 5.32e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 42.73  E-value: 5.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 213 SHYGNQNIANLLIQKG--ADVNYSAKHNISPLHVAAKWGKTNMVSLLLEKGGNIEAKTRDGLTPLHCAARSGHEQVVDML 290
Cdd:PHA02946  12 SLYAKYNSKNLDVFRNmlQAIEPSGNYHILHAYCGIKGLDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAML 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 291 LERGAPISAKTKNGLAPLHM--AAQGEHVDAARILLYHRAPVDEVTVDYLTALHVAAHCGHVRVAKLLLDRNADanARAL 368
Cdd:PHA02946  92 LTHGADPNACDKQHKTPLYYlsGTDDEVIERINLLVQYGAKINNSVDEEGCGPLLACTDPSERVFKKIMSIGFE--ARIV 169
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442630835 369 NGFTPLHI----ACKKNRLKVVELLLRHGASISATTESGLTPLHVAAFMGCMNI-VIYLLQHDASPDVPTVRGETPLHL 442
Cdd:PHA02946 170 DKFGKNHIhrhlMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCSKTVKNVdIINLLLPSTDVNKQNKFGDSPLTL 248
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
435-464 5.81e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.24  E-value: 5.81e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 442630835  435 RGETPLHLAARANQTDIIRILLRNGAQVDA 464
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
96-150 6.30e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.10  E-value: 6.30e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 442630835   96 LLEH-NASVNVQSQNGFTPLYMAAQENHDAVVRLLLSNGANQSLATEDGFTPLAVA 150
Cdd:pfam13857   1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
141-313 6.36e-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: 42.49  E-value: 6.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 141 EDGFTPLAVAMQQGHDK---VVAVLLEsdtrgkvrlpalhIAAKKDDVKAATllldNDHNPDVTSKsGFTPLHIASHYGN 217
Cdd:cd22196   45 ETGKTCLLKAMLNLHNGqndTISLLLD-------------IAEKTGNLKEFV----NAAYTDSYYK-GQTALHIAIERRN 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 218 QNIANLLIQKGADVNYSA-----KHNIS---------PLHVAAKWGKTNMVSLLLE---KGGNIEAKTRDGLTPLHCAAR 280
Cdd:cd22196  107 MHLVELLVQNGADVHARAsgeffKKKKGgpgfyfgelPLSLAACTNQLDIVKFLLEnphSPADISARDSMGNTVLHALVE 186
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 442630835 281 SGHEQVV---------DMLLERGAPISAK-------TKNGLAPLHMAAQ 313
Cdd:cd22196  187 VADNTPEntkfvtkmyNEILILGAKIRPLlkleeitNKKGLTPLKLAAK 235
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
66-293 6.58e-04

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 42.56  E-value: 6.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  66 RGAIVDSATKK---GNTALHIASL---AGQEEVVKLLLEH-----------NASVNVQSQNGFTPLYMAAQENHDAVVRL 128
Cdd:cd21882   12 RWYLTDSAYQRgatGKTCLHKAALnlnDGVNEAIMLLLEAapdsgnpkelvNAPCTDEFYQGQTALHIAIENRNLNLVRL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 129 LLSNGANQSL-ATEDGFtplavamqQGHDKVVAVLLEsdtrgkvrLPaLHIAAKKDDVKAATLLLDNDHNP---DVTSKS 204
Cdd:cd21882   92 LVENGADVSArATGRFF--------RKSPGNLFYFGE--------LP-LSLAACTNQEEIVRLLLENGAQPaalEAQDSL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 205 GFTPLHIASHYGNQNIANLLIQkgadvnysakhnisplhvaakwgkTNMVSLLLEKGGNI-------EAKTRDGLTPLHC 277
Cdd:cd21882  155 GNTVLHALVLQADNTPENSAFV------------------------CQMYNLLLSYGAHLdptqqleEIPNHQGLTPLKL 210
                        250
                 ....*....|....*.
gi 442630835 278 AARSGHEQVVDMLLER 293
Cdd:cd21882  211 AAVEGKIVMFQHILQR 226
PHA02884 PHA02884
ankyrin repeat protein; Provisional
352-525 7.20e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 41.89  E-value: 7.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 352 VAKLLLDRNADANAR---ALNGF-TPLHIACKKNRLKVVELLLRHGASISA-TTESGLTPLHVAAFMGCMNIVIYLLQHD 426
Cdd:PHA02884  48 IIDAILKLGADPEAPfplSENSKtNPLIYAIDCDNDDAAKLLIRYGADVNRyAEEAKITPLYISVLHGCLKCLEILLSYG 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 427 ASPDVPTVRGETPLHLAaranqtdiIRILLRNGAQVDARAREQQTPLHIASRLGNVDIVMLLLQHGAqVDATTKDMYTAL 506
Cdd:PHA02884 128 ADINIQTNDMVTPIELA--------LMICNNFLAFMICDNEISNFYKHPKKILINFDILKILVSHFI-LQASNDRLNEKH 198
                        170
                 ....*....|....*....
gi 442630835 507 HIAAKEGQDEVKDLIAKKI 525
Cdd:PHA02884 199 NKNFNAGYNKNKHLIIQSI 217
Ank_5 pfam13857
Ankyrin repeats (many copies);
63-117 7.44e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.71  E-value: 7.44e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 442630835   63 LLRRGAI-VDSATKKGNTALHIASLAGQEEVVKLLLEHNASVNVQSQNGFTPLYMA 117
Cdd:pfam13857   1 LLEHGPIdLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
76-105 1.02e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.47  E-value: 1.02e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 442630835   76 KGNTALHIASLAGQEEVVKLLLEHNASVNV 105
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
34-84 1.09e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.33  E-value: 1.09e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 442630835   34 NIDINTSNANGLNALHLASKDGHIHVVSELLRRGAIVDSATKKGNTALHIA 84
Cdd:pfam13857   6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
435-464 1.19e-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: 36.41  E-value: 1.19e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 442630835   435 RGETPLHLAARANQTDIIRILLRNGAQVDA 464
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
339-366 1.35e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.50  E-value: 1.35e-03
                          10        20
                  ....*....|....*....|....*....
gi 442630835  339 TALHVAA-HCGHVRVAKLLLDRNADANAR 366
Cdd:pfam00023   4 TPLHLAAgRRGNLEIVKLLLSKGADVNAR 32
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
109-135 1.43e-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: 36.41  E-value: 1.43e-03
                           10        20
                   ....*....|....*....|....*..
gi 442630835   109 NGFTPLYMAAQENHDAVVRLLLSNGAN 135
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
Ank_4 pfam13637
Ankyrin repeats (many copies);
112-163 1.77e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.48  E-value: 1.77e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 442630835  112 TPLYMAAQENHDAVVRLLLSNGANQSLATEDGFTPLAVAMQQGHDKVVAVLL 163
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
123-224 2.02e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.04  E-value: 2.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 123 DAV-VRLLLSNGANQSLATEDGFTPLAVAMQQGHDKVVAVLLESDTrgkvrlpalhiaakkddvkaatllldndhNPDVT 201
Cdd:PTZ00322  94 DAVgARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGA-----------------------------DPTLL 144
                         90       100
                 ....*....|....*....|...
gi 442630835 202 SKSGFTPLHIASHYGNQNIANLL 224
Cdd:PTZ00322 145 DKDGKTPLELAEENGFREVVQLL 167
PHA02736 PHA02736
Viral ankyrin protein; Provisional
354-463 2.11e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 39.09  E-value: 2.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 354 KLLLDRNADANAR-ALNGFTPLHIACKKNRLKVVELLLRhgasisattESGLTplhvaafmgcMNIVIYLLQhdaspdvp 432
Cdd:PHA02736  75 KLLMEWGADINGKeRVFGNTPLHIAVYTQNYELATWLCN---------QPGVN----------MEILNYAFK-------- 127
                         90       100       110
                 ....*....|....*....|....*....|.
gi 442630835 433 tvrgeTPLHLAARANQTDIIRILLRNGAQVD 463
Cdd:PHA02736 128 -----TPYYVACERHDAKMMNILRAKGAQCK 153
PHA02859 PHA02859
ankyrin repeat protein; Provisional
91-151 3.31e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 39.03  E-value: 3.31e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442630835  91 EVVKLLLEHNASVNVQSQ-NGFTPL--YMAAQEN-HDAVVRLLLSNGANQSLATEDGFTPLAVAM 151
Cdd:PHA02859  67 EILKFLIENGADVNFKTRdNNLSALhhYLSFNKNvEPEILKILIDSGSSITEEDEDGKNLLHMYM 131
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
336-365 3.51e-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: 35.31  E-value: 3.51e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 442630835  336 DYLTALHVAAHCGHVRVAKLLLDRNADANA 365
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
336-365 3.75e-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: 34.87  E-value: 3.75e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 442630835   336 DYLTALHVAAHCGHVRVAKLLLDRNADANA 365
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02884 PHA02884
ankyrin repeat protein; Provisional
329-423 4.04e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 39.58  E-value: 4.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 329 PVDEVTvdYLTALHVAAHCGHVRVAKLLLDRNADANARALNG-FTPLHIACKKNRLKVVELLLRHGASISATTESGLTPL 407
Cdd:PHA02884  64 PLSENS--KTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAkITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPI 141
                         90
                 ....*....|....*.
gi 442630835 408 HVAAfMGCMNIVIYLL 423
Cdd:PHA02884 142 ELAL-MICNNFLAFMI 156
PHA03095 PHA03095
ankyrin-like protein; Provisional
11-81 4.31e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 39.62  E-value: 4.31e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442630835  11 GNTSFLRAARAGNLER--VLEHLKNNIDINTSNANGLNALHLASKDGHIHVVSELLRRGAIVDSATKKGNTAL 81
Cdd:PHA03095 222 GNTPLHSMATGSSCKRslVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
471-497 5.46e-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: 5.46e-03
                           10        20
                   ....*....|....*....|....*..
gi 442630835   471 TPLHIASRLGNVDIVMLLLQHGAQVDA 497
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV4 cd22195
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed ...
76-250 6.49e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed broadly in neuronal and non-neuronal cells. It is activated by various stimuli, including hypo-osmolarity, warm temperature, and chemical ligands. TRPV4 acts in physiological functions such as osmoregulation and thermoregulation. It also has a role in mechanosensation in the vascular endothelium and urinary tract, and in cell barrier formation in vascular and epidermal tissues. Knockout mice studies suggested the functional importance of TRPV4 in the central nervous system, nociception, and bone formation. TRPV4 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: 411979 [Multi-domain]  Cd Length: 733  Bit Score: 39.45  E-value: 6.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835  76 KGNTALHIASLAGQEEVVKLLLEHNASVNVQSQNGF--------------TPLYMAAQENHDAVVRLLLSNganqslate 141
Cdd:cd22195  136 RGQTALHIAIERRCKHYVELLVEKGADVHAQARGRFfqpkdeggyfyfgeLPLSLAACTNQPDIVHYLTEN--------- 206
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 142 dgftplavamqqGHDKvvAVLLESDTRGKVRLPAL-HIAAK-KDDVKAATLLLDndhnpdvtsksgFTPLHIASHYGNQN 219
Cdd:cd22195  207 ------------AHKK--ADLRRQDSRGNTVLHALvAIADNtRENTKFVTKMYD------------LLLIKCAKLYPDCN 260
                        170       180       190
                 ....*....|....*....|....*....|.
gi 442630835 220 IANLLIQKGadvnysakhnISPLHVAAKWGK 250
Cdd:cd22195  261 LEAILNNDG----------MSPLMMAAKLGK 281
PHA02917 PHA02917
ankyrin-like protein; Provisional
75-123 6.72e-03

ankyrin-like protein; Provisional


Pssm-ID: 165231 [Multi-domain]  Cd Length: 661  Bit Score: 39.21  E-value: 6.72e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 442630835  75 KKGNTALHIASLAGQEEVVKLLLEHNASVNVQSQNGFTPLYMAAQENHD 123
Cdd:PHA02917 450 KRGETLLHKAVRYNKQSLVSLLLESGSDVNIRSNNGYTCIAIAINESRN 498
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
447-529 6.85e-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: 39.36  E-value: 6.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 447 NQTDIIRILL----RNG-------AQVDARAREQQTPLHIASRLGNVDIVMLLLQHGAQVDATTKDMY------------ 503
Cdd:cd22194  108 NTKEIVRILLafaeENGildrfinAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVFfnpkykhegfyf 187
                         90       100
                 ....*....|....*....|....*...
gi 442630835 504 --TALHIAAKEGQDEVKDLIAKKITDHI 529
Cdd:cd22194  188 geTPLALAACTNQPEIVQLLMEKESTDI 215
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
109-135 7.81e-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: 7.81e-03
                          10        20
                  ....*....|....*....|....*...
gi 442630835  109 NGFTPLYMAA-QENHDAVVRLLLSNGAN 135
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGAD 28
PHA02736 PHA02736
Viral ankyrin protein; Provisional
269-394 8.30e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 37.16  E-value: 8.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 269 RDGLTPLHCAARSGheQVVDMLLERGAPISAK-------TKNGLAPLHMAAQGEHVD---AARILLYHRAPVD-EVTVDY 337
Cdd:PHA02736  15 IEGENILHYLCRNG--GVTDLLAFKNAISDENrylvleyNRHGKQCVHIVSNPDKADpqeKLKLLMEWGADINgKERVFG 92
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 442630835 338 LTALHVAAHCGHVRVAKLLLdRNADANARALNGF--TPLHIACKKNRLKVVELLLRHGA 394
Cdd:PHA02736  93 NTPLHIAVYTQNYELATWLC-NQPGVNMEILNYAfkTPYYVACERHDAKMMNILRAKGA 150
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
403-433 8.71e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.19  E-value: 8.71e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 442630835  403 GLTPLHVAAFM-GCMNIVIYLLQHDASPDVPT 433
Cdd:pfam00023   2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
PHA02736 PHA02736
Viral ankyrin protein; Provisional
161-261 9.57e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 37.16  E-value: 9.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630835 161 VLLESDTRGKvrlPALHIAAKKDDVKAAT-LLLDNDHNPDVTSKS---GFTPLHIASHYGNQNIANLLI-QKGADV---N 232
Cdd:PHA02736  47 LVLEYNRHGK---QCVHIVSNPDKADPQEkLKLLMEWGADINGKErvfGNTPLHIAVYTQNYELATWLCnQPGVNMeilN 123
                         90       100
                 ....*....|....*....|....*....
gi 442630835 233 YSAKhniSPLHVAAKWGKTNMVSLLLEKG 261
Cdd:PHA02736 124 YAFK---TPYYVACERHDAKMMNILRAKG 149
 
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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