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Conserved domains on  [gi|1884823721|gb|KAF6215003|]
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hypothetical protein GE061_009751 [Apolygus lucorum]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
160-388 1.41e-48

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 170.91  E-value: 1.41e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 160 VDAQDPRGRCALHYAAEAGQLEAVEYLIEAGSKVDLGDRESLTPLHLAAVRGHLDVVKCLLKMKAHVNAKCTDKMTPLHY 239
Cdd:COG0666    47 LALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHL 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 240 SASRGHVDIVTTLISHGASVNTLDSGDRTPLKLAASRDLYQVVKVLVESNAKVNIEDVKGYTALCEAVWQKNVAMARLLL 319
Cdd:COG0666   127 AAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLL 206

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1884823721 320 EAGAKLTP------TPflLHYAILHRHSEMIELLLEAGAMVNIRDDHGSTPLIVAAVTAQPTIIRLLLKYGAQVD 388
Cdd:COG0666   207 EAGADVNAkdndgkTA--LDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLA 279
PLN03192 super family cl33658
Voltage-dependent potassium channel; Provisional
 332-458 4.58e-06

Voltage-dependent potassium channel; Provisional


The actual alignment was detected with superfamily member PLN03192:

Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 49.87  E-value: 4.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 332 LHYAILHRHSEMIELLLEAGAMVNIRDDHGSTPLIVAAVTAQPTIIRLLLKYGAQVD-FCGGlswktpllSVLQTDHIPT 410
Cdd:PLN03192  562 LHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDpHAAG--------DLLCTAAKRN 633

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1884823721 411 DLGVILELIMGGADVDKACWD-MTPLYATICHNKVDAANLLLRHGASVT 458
Cdd:PLN03192  634 DLTAMKELLKQGLNVDSEDHQgATALQVAMAEDHVDMVRLLIMNGADVD 682
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
 523-562 7.00e-04

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


:

Pssm-ID: 462192  Cd Length: 39  Bit Score: 37.53  E-value: 7.00e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1884823721 523 PLKLSELARIKIRSLWPRRCSmaDYVRSLGLPRLLEEYLL 562
Cdd:pfam07525   2 PRSLQHLCRLAIRRALGKRRL--GAIDKLPLPPLLKDYLL 39
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
160-388 1.41e-48

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 170.91  E-value: 1.41e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 160 VDAQDPRGRCALHYAAEAGQLEAVEYLIEAGSKVDLGDRESLTPLHLAAVRGHLDVVKCLLKMKAHVNAKCTDKMTPLHY 239
Cdd:COG0666    47 LALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHL 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 240 SASRGHVDIVTTLISHGASVNTLDSGDRTPLKLAASRDLYQVVKVLVESNAKVNIEDVKGYTALCEAVWQKNVAMARLLL 319
Cdd:COG0666   127 AAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLL 206

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1884823721 320 EAGAKLTP------TPflLHYAILHRHSEMIELLLEAGAMVNIRDDHGSTPLIVAAVTAQPTIIRLLLKYGAQVD 388
Cdd:COG0666   207 EAGADVNAkdndgkTA--LDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLA 279
Ank_2 pfam12796
Ankyrin repeats (3 copies);
171-263 1.91e-25

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 100.19  E-value: 1.91e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 171 LHYAAEAGQLEAVEYLIEAGSKVDLGDRESLTPLHLAAVRGHLDVVKCLLKmKAHVNAKCtDKMTPLHYSASRGHVDIVT 250
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1884823721 251 TLISHGASVNTLD 263
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 179-492 2.79e-24

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 107.46  E-value: 2.79e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 179 QLEAVEYLIEAGSKVDLGDRESLTPLHLAAVRGHLDVVKCLLKMKAHVNAKCTDKMTPLHYSASRGHVDIVTTLISH--- 255
Cdd:PHA02876  157 ELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNrsn 236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 256 --------------------------GASVNTLDSGDRTPLKLAA-SRDLYQVVKVLVESNAKVNIEDVKGYTALceAVW 308
Cdd:PHA02876  237 inkndlsllkairnedletslllydaGFSVNSIDDCKNTPLHHASqAPSLSRLVPKLLERGADVNAKNIKGETPL--YLM 314

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 309 QKN---VAMARLLLEAGAKLTPTPFL----LHYA-ILHRHSEMIELLLEAGAMVNIRDDHGSTPLIVAAVTAQPTIIRLL 380
Cdd:PHA02876  315 AKNgydTENIRTLIMLGADVNAADRLyitpLHQAsTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTL 394

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 381 LKYGAQVDfcgGLSWKtpLLSVLQTDHIPTD-LGVILELIMGGADVDKACWDM-TPL-YATICHNKVDAANLLLRHGASV 457
Cdd:PHA02876  395 LDYGADIE---ALSQK--IGTALHFALCGTNpYMSVKTLIDRGANVNSKNKDLsTPLhYACKKNCKLDVIEMLLDNGADV 469

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1884823721 458 TTrPGVRSHDPMIIArrIGALPIVQTLVLCGYDLQ 492
Cdd:PHA02876  470 NA-INIQNQYPLLIA--LEYHGIVNILLHYGAELR 501
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 258-406 4.74e-09

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: 59.32  E-value: 4.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 258 SVNTLDSGDRTPLKLAASRDLYQVVKVLVESNakvNIEDVKGYTALCEAV--WQKNVAMARLLLEAGAKLTPTPFL---- 331
Cdd:TIGR00870  44 NINCPDRLGRSALFVAAIENENLELTELLLNL---SCRGAVGDTLLHAISleYVDAVEAILLHLLAAFRKSGPLELandq 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 332 -----------LHYAILHRHSEMIELLLEAGAMVNIR---DD-----------HGSTPLIVAAVTAQPTIIRLLLKYGAQ 386
Cdd:TIGR00870 121 ytseftpgitaLHLAAHRQNYEIVKLLLERGASVPARacgDFfvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPAD 200

                         170       180
                  ....*....|....*....|
gi 1884823721 387 VDFCGGLSWKTPLLSVLQTD 406
Cdd:TIGR00870 201 ILTADSLGNTLLHLLVMENE 220
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 157-270 5.89e-08

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 55.79  E-value: 5.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 157 CSRVD--AQDPRGRCALHYAAEAGQLEAVEYLIEAGSKV-------DLgdRESLTPLHLAAVRGHLDVVKCLLKMKAHV- 226
Cdd:cd22192    39 CPSCDlfQRGALGETALHVAALYDNLEAAVVLMEAAPELvnepmtsDL--YQGETALHIAVVNQNLNLVRELIARGADVv 116

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1884823721 227 NAKCTDKM-------------TPLHYSASRGHVDIVTTLISHGASVNTLDSGDRTPL 270
Cdd:cd22192   117 SPRATGTFfrpgpknliyygeHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 332-458 4.58e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 49.87  E-value: 4.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 332 LHYAILHRHSEMIELLLEAGAMVNIRDDHGSTPLIVAAVTAQPTIIRLLLKYGAQVD-FCGGlswktpllSVLQTDHIPT 410
Cdd:PLN03192  562 LHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDpHAAG--------DLLCTAAKRN 633

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1884823721 411 DLGVILELIMGGADVDKACWD-MTPLYATICHNKVDAANLLLRHGASVT 458
Cdd:PLN03192  634 DLTAMKELLKQGLNVDSEDHQgATALQVAMAEDHVDMVRLLIMNGADVD 682
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 232-260 1.26e-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: 1.26e-05
                           10        20
                   ....*....|....*....|....*....
gi 1884823721  232 DKMTPLHYSASRGHVDIVTTLISHGASVN 260
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
 523-562 7.00e-04

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


Pssm-ID: 462192  Cd Length: 39  Bit Score: 37.53  E-value: 7.00e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1884823721 523 PLKLSELARIKIRSLWPRRCSmaDYVRSLGLPRLLEEYLL 562
Cdd:pfam07525   2 PRSLQHLCRLAIRRALGKRRL--GAIDKLPLPPLLKDYLL 39
SOCS cd03587
SOCS (suppressors of cytokine signaling) box. The SOCS box is found in the C-terminal region ...
 523-562 2.05e-03

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


Pssm-ID: 239641  Cd Length: 41  Bit Score: 36.29  E-value: 2.05e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1884823721 523 PLKLSELARIKIRSLWPRRCsmADYVRSLGLPRLLEEYLL 562
Cdd:cd03587     2 PRSLQHLCRLAIRRCLGKRR--LDLIDKLPLPPRLKDYLL 39
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
160-388 1.41e-48

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 170.91  E-value: 1.41e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 160 VDAQDPRGRCALHYAAEAGQLEAVEYLIEAGSKVDLGDRESLTPLHLAAVRGHLDVVKCLLKMKAHVNAKCTDKMTPLHY 239
Cdd:COG0666    47 LALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHL 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 240 SASRGHVDIVTTLISHGASVNTLDSGDRTPLKLAASRDLYQVVKVLVESNAKVNIEDVKGYTALCEAVWQKNVAMARLLL 319
Cdd:COG0666   127 AAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLL 206

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1884823721 320 EAGAKLTP------TPflLHYAILHRHSEMIELLLEAGAMVNIRDDHGSTPLIVAAVTAQPTIIRLLLKYGAQVD 388
Cdd:COG0666   207 EAGADVNAkdndgkTA--LDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLA 279
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
160-365 2.24e-47

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 167.82  E-value: 2.24e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 160 VDAQDPRGRCALHYAAEAGQLEAVEYLIEAGSKVDLGDRESLTPLHLAAVRGHLDVVKCLLKMKAHVNAKCTDKMTPLHY 239
Cdd:COG0666    80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 240 SASRGHVDIVTTLISHGASVNTLDSGDRTPLKLAASRDLYQVVKVLVESNAKVNIEDVKGYTALCEAVWQKNVAMARLLL 319
Cdd:COG0666   160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1884823721 320 EAGAKLTPTPF----LLHYAILHRHSEMIELLLEAGAMVNIRDDHGSTPL 365
Cdd:COG0666   240 EAGADLNAKDKdgltALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
170-428 4.27e-47

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 167.05  E-value: 4.27e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 170 ALHYAAEAGQLEAVEYLIEAGSKVDLGDRESLTPLHLAAVRGHLDVVKCLLKMKAHVNAKCTDKMTPLHYSASRGHVDIV 249
Cdd:COG0666    24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIV 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 250 TTLISHGASVNTLDSGDRTPLKLAASRDLYQVVKVLVESNAKVNIEDVKGYTALCEAVWQKNVAMARLLLEAGAKL---- 325
Cdd:COG0666   104 KLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVnard 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 326 ----TPtpflLHYAILHRHSEMIELLLEAGAMVNIRDDHGSTPLIVAAVTAQPTIIRLLLKYGAQVDFCGGLSWKTPLLS 401
Cdd:COG0666   184 ndgeTP----LHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLA 259

                         250       260
                  ....*....|....*....|....*..
gi 1884823721 402 VLQTDHIPTDLGVILELIMGGADVDKA 428
Cdd:COG0666   260 AAAGAALIVKLLLLALLLLAAALLDLL 286
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
180-455 3.01e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 148.18  E-value: 3.01e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 180 LEAVEYLIEAGSKVDLGDRESLTPLHLAAVRGHLDVVKCLLKMKAHVNAKCTDKMTPLHYSASRGHVDIVTTLISHGASV 259
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 260 NTLDSGDRTPLKLAASRDLYQVVKVLVESNAKVNIEDVKGYTALCEAVWQKNVAMARLLLEAGAKL--------TPtpfl 331
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVnaqdndgnTP---- 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 332 LHYAILHRHSEMIELLLEAGAMVNIRDDHGSTPLIVAAVTAQPTIIRLLLKYGAQVDFCgGLSWKTPLLSVLQTDHIPTd 411
Cdd:COG0666   157 LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAK-DNDGKTALDLAAENGNLEI- 234

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1884823721 412 lgVILELIMGGADVDKACWDMTPLYATICHNKVDAANLLLRHGA 455
Cdd:COG0666   235 --VKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALL 276
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
25-325 1.68e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 123.91  E-value: 1.68e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721  25 LAIAVSQKDFEKVHHLLLQGVNknglfkgktllsvaasegdvntmrvlletiqetpveeassilpppgnngyfvvvrege 104
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGAD---------------------------------------------------------- 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 105 ddanssrhrfrtkseevttpegmadlqwdteleeispvpdkvrqvevdtgnscsrVDAQDPRGRCALHYAAEAGQLEAVE 184
Cdd:COG0666   113 -------------------------------------------------------VNARDKDGETPLHLAAYNGNLEIVK 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 185 YLIEAGSKVDLGDRESLTPLHLAAVRGHLDVVKCLLKMKAHVNAKCTDKMTPLHYSASRGHVDIVTTLISHGASVNTLDS 264
Cdd:COG0666   138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN 217

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1884823721 265 GDRTPLKLAASRDLYQVVKVLVESNAKVNIEDVKGYTALCEAVWQKNVAMARLLLEAGAKL 325
Cdd:COG0666   218 DGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278
Ank_2 pfam12796
Ankyrin repeats (3 copies);
171-263 1.91e-25

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 100.19  E-value: 1.91e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 171 LHYAAEAGQLEAVEYLIEAGSKVDLGDRESLTPLHLAAVRGHLDVVKCLLKmKAHVNAKCtDKMTPLHYSASRGHVDIVT 250
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1884823721 251 TLISHGASVNTLD 263
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 179-492 2.79e-24

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 107.46  E-value: 2.79e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 179 QLEAVEYLIEAGSKVDLGDRESLTPLHLAAVRGHLDVVKCLLKMKAHVNAKCTDKMTPLHYSASRGHVDIVTTLISH--- 255
Cdd:PHA02876  157 ELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNrsn 236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 256 --------------------------GASVNTLDSGDRTPLKLAA-SRDLYQVVKVLVESNAKVNIEDVKGYTALceAVW 308
Cdd:PHA02876  237 inkndlsllkairnedletslllydaGFSVNSIDDCKNTPLHHASqAPSLSRLVPKLLERGADVNAKNIKGETPL--YLM 314

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 309 QKN---VAMARLLLEAGAKLTPTPFL----LHYA-ILHRHSEMIELLLEAGAMVNIRDDHGSTPLIVAAVTAQPTIIRLL 380
Cdd:PHA02876  315 AKNgydTENIRTLIMLGADVNAADRLyitpLHQAsTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTL 394

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 381 LKYGAQVDfcgGLSWKtpLLSVLQTDHIPTD-LGVILELIMGGADVDKACWDM-TPL-YATICHNKVDAANLLLRHGASV 457
Cdd:PHA02876  395 LDYGADIE---ALSQK--IGTALHFALCGTNpYMSVKTLIDRGANVNSKNKDLsTPLhYACKKNCKLDVIEMLLDNGADV 469

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1884823721 458 TTrPGVRSHDPMIIArrIGALPIVQTLVLCGYDLQ 492
Cdd:PHA02876  470 NA-INIQNQYPLLIA--LEYHGIVNILLHYGAELR 501
PHA03095 PHA03095
ankyrin-like protein; Provisional
 164-388 3.36e-24

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 105.88  E-value: 3.36e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 164 DPRGRCALH-YAAEAGQ--LEAVEYLIEAGSKVDLGDRESLTPLHLAAVRGH-LDVVKCLLKMKAHVNAKCTDKMTPLH- 238
Cdd:PHA03095   44 GEYGKTPLHlYLHYSSEkvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGADVNAKDKVGRTPLHv 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 239 YSAS-RGHVDIVTTLISHGASVNTLDSGDRTPLK-LAASRDL-YQVVKVLVESNAKVNIEDVKGYTAL---CEAVwQKNV 312
Cdd:PHA03095  124 YLSGfNINPKVIRLLLRKGADVNALDLYGMTPLAvLLKSRNAnVELLRLLIDAGADVYAVDDRFRSLLhhhLQSF-KPRA 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 313 AMARLLLEAGAKLTPTPFL----LHYAILH---RHSEMIELLlEAGAMVNIRDDHGSTPLIVAAVTAQPTIIRLLLKYGA 385
Cdd:PHA03095  203 RIVRELIRAGCDPAATDMLgntpLHSMATGsscKRSLVLPLL-IAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGA 281


                  ...
gi 1884823721 386 QVD 388
Cdd:PHA03095  282 DIN 284
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 171-389 6.27e-24

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 104.36  E-value: 6.27e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 171 LHYAAEAGQLEAVEYLIEAGSKVDLGDRESLTPLHLAAVRGH-----LDVVKCLLKMKAHVNAKCTDKMTPLHYSASR-- 243
Cdd:PHA03100   39 LYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITPLLYAISKks 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 244 GHVDIVTTLISHGASVNTLDSGDRTPLKLAAS---RDLyQVVKVLVESNAKVNIED-VKgytalceavwqknvamarLLL 319
Cdd:PHA03100  119 NSYSIVEYLLDNGANVNIKNSDGENLLHLYLEsnkIDL-KILKLLIDKGVDINAKNrVN------------------YLL 179

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1884823721 320 EAGAKL--------TPtpflLHYAILHRHSEMIELLLEAGAMVNIRDDHGSTPLIVAAVTAQPTIIRLLLKYGAQVDF 389
Cdd:PHA03100  180 SYGVPInikdvygfTP----LHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 180-390 1.05e-22

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 100.89  E-value: 1.05e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 180 LEAVEYLIEAGSKVDLGDRESLTPLHLAAVRGHLDVVKCLLKMKAHVNAKCTDKMTPLHYSASRGHV-----DIVTTLIS 254
Cdd:PHA03100   15 VKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLE 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 255 HGASVNTLDSGDRTPLKLAASRDL--YQVVKVLVESNAKVNIEDVKGYTALCEAVWQK--NVAMARLLLEAGAKLTptpf 330
Cdd:PHA03100   95 YGANVNAPDNNGITPLLYAISKKSnsYSIVEYLLDNGANVNIKNSDGENLLHLYLESNkiDLKILKLLIDKGVDIN---- 170

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 331 llhyaILHRhsemIELLLEAGAMVNIRDDHGSTPLIVAAVTAQPTIIRLLLKYGAQVDFC 390
Cdd:PHA03100  171 -----AKNR----VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLV 221
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 161-323 9.20e-22

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 97.75  E-value: 9.20e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 161 DAQDPRGRCALHYAAEAGQLEAVEYLIEAGSKV-DLGDRESLTPLHLAAVRGHLDVVKCLLKMKAHVNAKCTDKMTPLHY 239
Cdd:PHA02875   62 DVKYPDIESELHDAVEEGDVKAVEELLDLGKFAdDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHL 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 240 SASRGHVDIVTTLISHGASVNTLDSGDRTPLKLAASRDLYQVVKVLVESNAKVNIEDVKG-YTALCEAVWQKNVAMARLL 318
Cdd:PHA02875  142 AVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLF 221


                  ....*
gi 1884823721 319 LEAGA 323
Cdd:PHA02875  222 IKRGA 226
Ank_2 pfam12796
Ankyrin repeats (3 copies);
204-296 1.25e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.40  E-value: 1.25e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 204 LHLAAVRGHLDVVKCLLKMKAHVNAKCTDKMTPLHYSASRGHVDIVTTLISHgASVNTLDSGdRTPLKLAASRDLYQVVK 283
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG-RTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1884823721 284 VLVESNAKVNIED 296
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 139-368 1.71e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 91.18  E-value: 1.71e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 139 ISPVPDkVRQVEVDTGNSCS-RVDAQDPRGRCALHYAAEAGQLEAVEYLIEAGSKVDLGDRESLTPLHLAAVRGHLDVVK 217
Cdd:PHA02874   96 ILPIPC-IEKDMIKTILDCGiDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIK 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 218 CLLKMKAHVNAKCTDKMTPLHYSASRGHVDIVTTLISHGASVNTLDSGDRTPLKLAASRDlYQVVKVLVeSNAKVNIEDV 297
Cdd:PHA02874  175 LLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHN-RSAIELLI-NNASINDQDI 252

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1884823721 298 KGYTAlceavwqknvamarllleagakltptpflLHYAILHRHS-EMIELLLEAGAMVNIRDDHGSTPLIVA 368
Cdd:PHA02874  253 DGSTP-----------------------------LHHAINPPCDiDIIDILLYHKADISIKDNKGENPIDTA 295
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 160-387 4.03e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 91.28  E-value: 4.03e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 160 VDAQDPRGRCALHYAAEAG-QLEAVEYLIEAGSKVDLGDRESLTPLHLAA-VRGHLDVVKCLLKMKAHVNAKCTDKMTPL 237
Cdd:PHA02876  300 VNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQAStLDRNKDIVITLLELGANVNARDYCDKTPI 379

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 238 HYSASRGHVDIVTTLISHGASVNTLDSGDRTPLKLA-ASRDLYQVVKVLVESNAKVNiedvkgytalceavwQKNvamar 316
Cdd:PHA02876  380 HYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVN---------------SKN----- 439

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1884823721 317 llleagaKLTPTPflLHYAILHR-HSEMIELLLEAGAMVNIRDDHGSTPLIVAavTAQPTIIRLLLKYGAQV 387
Cdd:PHA02876  440 -------KDLSTP--LHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIA--LEYHGIVNILLHYGAEL 500
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 171-371 1.70e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 88.40  E-value: 1.70e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 171 LHYAAEAGQLEAVEYLIEAGSKVDLGDRESLTPLHLAAVRGHL------------------------------------- 213
Cdd:PHA02878   41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKlgmkemirsinkcsvfytlvaikdafnnrnveifkii 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 214 ---------------------------DVVKCLLKMKAHVNAKCTDKM-TPLHYSASRGHVDIVTTLISHGASVNTLDSG 265
Cdd:PHA02878  121 ltnrykniqtidlvyidkkskddiieaEITKLLLSYGADINMKDRHKGnTALHYATENKDQRLTELLLSYGANVNIPDKT 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 266 DRTPLKLAASRDLYQVVKVLVESNAKVNIEDVKGYTALCEAV-WQKNVAMARLLLEAGAKLTPTPFLLHYAILH---RHS 341
Cdd:PHA02878  201 NNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVgYCKDYDILKLLLEHGVDVNAKSYILGLTALHssiKSE 280

                         250       260       270
                  ....*....|....*....|....*....|
gi 1884823721 342 EMIELLLEAGAMVNIRDDHGSTPLIVAAVT 371
Cdd:PHA02878  281 RKLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 207-424 2.56e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 84.27  E-value: 2.56e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 207 AAVRGHLDVVKCLLKMKAHVNAKCTDKMTPLHYSASRGHVDIVTTLISHGASVNTLDSGDRTPLKLAASRDLYQVVKVLV 286
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 287 ESNAKVNieDV---KGYTALCEAVWQKNVAMARLLLEAGA--------KLTPtpflLHYAILHRHSEMIELLLEAGAMVN 355
Cdd:PHA02875   89 DLGKFAD--DVfykDGMTPLHLATILKKLDIMKLLIARGAdpdipntdKFSP----LHLAVMMGDIKGIELLIDHKACLD 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1884823721 356 IRDDHGSTPLIVAAVTAQPTIIRLLLKYGAQVDFCGGLSWKTPLLSVLQTDHIptdlGVILELIMGGAD 424
Cdd:PHA02875  163 IEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKI----DIVRLFIKRGAD 227
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 174-365 7.31e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 83.09  E-value: 7.31e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 174 AAEAGQLEAVEYLIEAGSKVDLGDRESLTPLHLA-AVRGH----------------------LDVVKCLLKMKAHVNAKC 230
Cdd:PHA02874   42 AIRSGDAKIVELFIKHGADINHINTKIPHPLLTAiKIGAHdiikllidngvdtsilpipcieKDMIKTILDCGIDVNIKD 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 231 TDKMTPLHYSASRGHVDIVTTLISHGASVNTLDSGDRTPLKLAASRDLYQVVKVLVESNAKVNIEDVKGYTALCEAVWQK 310
Cdd:PHA02874  122 AELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYG 201

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1884823721 311 NVAMARLLLEAGAKLTP------TPflLHYAILHRHSeMIELLLEaGAMVNIRDDHGSTPL 365
Cdd:PHA02874  202 DYACIKLLIDHGNHIMNkckngfTP--LHNAIIHNRS-AIELLIN-NASINDQDIDGSTPL 258
Ank_2 pfam12796
Ankyrin repeats (3 copies);
237-326 9.67e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.54  E-value: 9.67e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 237 LHYSASRGHVDIVTTLISHGASVNTLDSGDRTPLKLAASRDLYQVVKVLVEsNAKVNIEDvKGYTALCEAVWQKNVAMAR 316
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|
gi 1884823721 317 LLLEAGAKLT 326
Cdd:pfam12796  79 LLLEKGADIN 88
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 177-485 1.07e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 82.70  E-value: 1.07e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 177 AGQLEAVEYLIEA-GSKVDLGDRESLTPLHLAAVRGHLDVVKCLLKMKAHVNAKCTDKMTPLHYSASRGHVDIVTTLISH 255
Cdd:PHA02874   11 SGDIEAIEKIIKNkGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDN 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 256 GASVNTLDSGDRTPlklaasrdlyQVVKVLVESNAKVNIEDVKGYTALCEAVWQKNVAMARLLLEAGAKLTPTP----FL 331
Cdd:PHA02874   91 GVDTSILPIPCIEK----------DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDdngcYP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 332 LHYAILHRHSEMIELLLEAGAMVNIRDDHGSTPLIVAAVTAQPTIIRLLLKYGAQVDF-CG-GLswkTPLLSVLQTDHIP 409
Cdd:PHA02874  161 IHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNkCKnGF---TPLHNAIIHNRSA 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 410 TDLgVILELIMGGADVDKAcwdmTPLYATI---ChnKVDAANLLLRHGASVTTRPGvRSHDPMIIA-RRIGALPIVQTLV 485
Cdd:PHA02874  238 IEL-LINNASINDQDIDGS----TPLHHAInppC--DIDIIDILLYHKADISIKDN-KGENPIDTAfKYINKDPVIKDII 309
PHA03095 PHA03095
ankyrin-like protein; Provisional
 193-467 2.20e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 81.99  E-value: 2.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 193 VDLGDRESLTPLHLAAVRGHLDVVKCLLKMKAHVNAKCTDKMTPLHYSASRGH---VDIVTTLISHGASVNTLDSGDRTP 269
Cdd:PHA03095    7 VDIIMEAALYDYLLNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 270 LKL-AASRDLYQVVKVLVESNAKVNIEDVKGYTAL--CEAVWQKNVAMARLLLEAGAKLTPTPFLLHYAI---LHRHS-- 341
Cdd:PHA03095   87 LHLyLYNATTLDVIKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLavlLKSRNan 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 342 -EMIELLLEAGAMVNIRDDHGSTPLIVAAVTAQP--TIIRLLLKYG---AQVDFCGglswKTPLLSVlqTDHIPTDLGVI 415
Cdd:PHA03095  167 vELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPraRIVRELIRAGcdpAATDMLG----NTPLHSM--ATGSSCKRSLV 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1884823721 416 LELIMGGADVDKA-CWDMTPLYATICHNKVDAANLLLRHGASVTtrpgVRSHD 467
Cdd:PHA03095  241 LPLLIAGISINARnRYGQTPLHYAAVFNNPRACRRLIALGADIN----AVSSD 289
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 168-385 3.62e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 77.72  E-value: 3.62e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 168 RCALHYAAEAGQLEAVEYLIEAGSKVDLGDRESLTPLHLAAVRGHLDVVKCLLKMKAHVNAKCTDKMTPLHYSASRGHVD 247
Cdd:PHA02875    3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 248 IVTTLISHGASVNTLDSGD-RTPLKLAASRDLYQVVKVLVESNAKVNIEDVKGYTALCEAVWQKNVAMARLLLEAGAKLT 326
Cdd:PHA02875   83 AVEELLDLGKFADDVFYKDgMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLD 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1884823721 327 P------TPFLlhYAILHRHSEMIELLLEAGAMVNIRDDHGSTPLIVAAV-TAQPTIIRLLLKYGA 385
Cdd:PHA02875  163 IedccgcTPLI--IAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIeNNKIDIVRLFIKRGA 226
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 201-435 9.99e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 76.84  E-value: 9.99e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 201 LTPLHLAAVRGHLDVVKCLLKMKAHVNAKCTDKMTPLHYSASRGHVDIVTTLIS------------------HGASVNTL 262
Cdd:PHA02878   38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRsinkcsvfytlvaikdafNNRNVEIF 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 263 DSGDRTPLKLAASRDLYQ-------------VVKVLVESNAKVNIEDV-KGYTALCEAVWQKNVAMARLLLEAGAKLT-- 326
Cdd:PHA02878  118 KIILTNRYKNIQTIDLVYidkkskddiieaeITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNip 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 327 ----PTPflLHYAILHRHSEMIELLLEAGAMVNIRDDHGSTPL-IVAAVTAQPTIIRLLLKYGAQVDFCGGLSWKTPLLS 401
Cdd:PHA02878  198 dktnNSP--LHHAVKHYNKPIVHILLENGASTDARDKCGNTPLhISVGYCKDYDILKLLLEHGVDVNAKSYILGLTALHS 275

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1884823721 402 VLqtdHIPTDLGVILELimgGADVDKACWD-MTPL 435
Cdd:PHA02878  276 SI---KSERKLKLLLEY---GADINSLNSYkLTPL 304
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 166-309 9.99e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 76.84  E-value: 9.99e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 166 RGRCALHYAAEAGQLEAVEYLIEAGSKVDLGDRESLTPLHLAAVRGHLDVVKCLLKMKAHVNAKCTDKMTPLHYSASR-G 244
Cdd:PHA02878  167 KGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcK 246

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1884823721 245 HVDIVTTLISHGASVNTLDS-GDRTPLKLAASRDlyQVVKVLVESNAKVNIEDVKGYTALCEAVWQ 309
Cdd:PHA02878  247 DYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSE--RKLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
Ank_2 pfam12796
Ankyrin repeats (3 copies);
155-229 2.35e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.60  E-value: 2.35e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1884823721 155 NSCSRVDAQDPRGRCALHYAAEAGQLEAVEYLIEagsKVDLGDRES-LTPLHLAAVRGHLDVVKCLLKMKAHVNAK 229
Cdd:pfam12796  18 ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE---HADVNLKDNgRTALHYAARSGHLEIVKLLLEKGADINVK 90
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 164-326 1.22e-13

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 74.13  E-value: 1.22e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 164 DPRGRCALHYAAEAGQLEAVEYLIEAGSKVDLGDRESLTPLHLAAVRGHLDVVKCLLKMKAHVNAKCTDKMTPLHYSASR 243
Cdd:PLN03192  522 DPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISA 601

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 244 GHVDIVTTLISHGASVNTLDSGDRtpLKLAASRDLYQVVKVLVESNAKVNIEDVKGYTALCEAVWQKNVAMARLLLEAGA 323
Cdd:PLN03192  602 KHHKIFRILYHFASISDPHAAGDL--LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGA 679


                  ...
gi 1884823721 324 KLT 326
Cdd:PLN03192  680 DVD 682
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 236-474 1.33e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 73.38  E-value: 1.33e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 236 PLHYSASRGHVDIVTTLISHGASVNTLDSGDRTPLKLAASRDLYQVVKVLVESNAKVNIEDVkgYTALCEAVWQKNVAMA 315
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFYT--LVAIKDAFNNRNVEIF 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 316 RLLLEAGAKLTPTPFLLHYAILHR----HSEMIELLLEAGAMVNIRDDH-GSTPLIVAAVTAQPTIIRLLLKYGAQV--- 387
Cdd:PHA02878  118 KIILTNRYKNIQTIDLVYIDKKSKddiiEAEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVnip 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 388 DFCGglswKTPLLSVLQTDHIPtdlgVILELIMGGADVD-KACWDMTPLYATICHNK-VDAANLLLRHGASVTTRPGVRS 465
Cdd:PHA02878  198 DKTN----NSPLHHAVKHYNKP----IVHILLENGASTDaRDKCGNTPLHISVGYCKdYDILKLLLEHGVDVNAKSYILG 269


                  ....*....
gi 1884823721 466 HDPMIIARR 474
Cdd:PHA02878  270 LTALHSSIK 278
PHA03095 PHA03095
ankyrin-like protein; Provisional
 159-382 2.11e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 69.28  E-value: 2.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 159 RVDAQDPRGRCALHYAAEAGQ-LEAVEYLIEAGSKVDLGDRESLTPLH--LAAVRGHLDVVKCLLKMKAHVNAKCTDKMT 235
Cdd:PHA03095   75 DVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMT 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 236 PLH-YSASRG-HVDIVTTLISHGASV-------NTL----------------------------DSGDRTPLKLAA--SR 276
Cdd:PHA03095  155 PLAvLLKSRNaNVELLRLLIDAGADVyavddrfRSLlhhhlqsfkprarivreliragcdpaatDMLGNTPLHSMAtgSS 234

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 277 DLYQVVKVLVESNAKVNIEDVKGYTAlceavwqknvamarllleagakltptpflLHYAILHRHSEMIELLLEAGAMVNI 356
Cdd:PHA03095  235 CKRSLVLPLLIAGISINARNRYGQTP-----------------------------LHYAAVFNNPRACRRLIALGADINA 285

                         250       260
                  ....*....|....*....|....*.
gi 1884823721 357 RDDHGSTPLIVAAVTAQPTIIRLLLK 382
Cdd:PHA03095  286 VSSDGNTPLSLMVRNNNGRAVRAALA 311
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 183-264 1.52e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 66.61  E-value: 1.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 183 VEYLIEAGSKVDLGDRESLTPLHLAAVRGHLDVVKCLLKMKAHVNAKCTDKMTPLHYSASRGHVDIVTTLISHGASVNTL 262
Cdd:PHA03100  175 VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTI 254


                  ..
gi 1884823721 263 DS 264
Cdd:PHA03100  255 IE 256
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 241-388 2.63e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 66.43  E-value: 2.63e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 241 ASRGHVDIVTTLISHGASVNTLDSGDRTPLKLAASRDLYQVVKVLVESNAKVNIEDVKGYTALCEAVWQKNVAMARLLLE 320
Cdd:PLN03192  533 ASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYH 612

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 321 AGAKLTPTPF--LLHYAILHRHSEMIELLLEAGAMVNIRDDHGSTPLIVAAVTAQPTIIRLLLKYGAQVD 388
Cdd:PLN03192  613 FASISDPHAAgdLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVD 682
Ank_4 pfam13637
Ankyrin repeats (many copies);
201-253 3.32e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.44  E-value: 3.32e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1884823721 201 LTPLHLAAVRGHLDVVKCLLKMKAHVNAKCTDKMTPLHYSASRGHVDIVTTLI 253
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
332-460 5.39e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 59.36  E-value: 5.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 332 LHYAILHRHSEMIELLLEAGAMVNIRDDHGSTPLIVAAVTAQPTIIRLLLKYgaqvdfcgglswktpllsvlqtdhiptd 411
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH---------------------------- 52

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1884823721 412 lgvilelimggADVDKACWDMTPLYATICHNKVDAANLLLRHGASVTTR 460
Cdd:pfam12796  53 -----------ADVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVK 90
Ank_4 pfam13637
Ankyrin repeats (many copies);
170-220 2.64e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.13  E-value: 2.64e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1884823721 170 ALHYAAEAGQLEAVEYLIEAGSKVDLGDRESLTPLHLAAVRGHLDVVKCLL 220
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 258-406 4.74e-09

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: 59.32  E-value: 4.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 258 SVNTLDSGDRTPLKLAASRDLYQVVKVLVESNakvNIEDVKGYTALCEAV--WQKNVAMARLLLEAGAKLTPTPFL---- 331
Cdd:TIGR00870  44 NINCPDRLGRSALFVAAIENENLELTELLLNL---SCRGAVGDTLLHAISleYVDAVEAILLHLLAAFRKSGPLELandq 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 332 -----------LHYAILHRHSEMIELLLEAGAMVNIR---DD-----------HGSTPLIVAAVTAQPTIIRLLLKYGAQ 386
Cdd:TIGR00870 121 ytseftpgitaLHLAAHRQNYEIVKLLLERGASVPARacgDFfvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPAD 200

                         170       180
                  ....*....|....*....|
gi 1884823721 387 VDFCGGLSWKTPLLSVLQTD 406
Cdd:TIGR00870 201 ILTADSLGNTLLHLLVMENE 220
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 128-292 1.78e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 57.38  E-value: 1.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 128 ADLQWDTELEEISPVpDKVRQVEVDTGNSCSRVDAQDPRGRCALHYAAEAGQLEAVEYLIEAGSKVDLGDRESLTPLHLA 207
Cdd:PHA02876  337 ADRLYITPLHQASTL-DRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFA 415

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 208 AVRGH-LDVVKCLLKMKAHVNAKCTDKMTPLHYSASRG-HVDIVTTLISHGASVNTLDSGDRTPLKLAAsrDLYQVVKVL 285
Cdd:PHA02876  416 LCGTNpYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNIL 493


                  ....*..
gi 1884823721 286 VESNAKV 292
Cdd:PHA02876  494 LHYGAEL 500
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 157-270 5.89e-08

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 55.79  E-value: 5.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 157 CSRVD--AQDPRGRCALHYAAEAGQLEAVEYLIEAGSKV-------DLgdRESLTPLHLAAVRGHLDVVKCLLKMKAHV- 226
Cdd:cd22192    39 CPSCDlfQRGALGETALHVAALYDNLEAAVVLMEAAPELvnepmtsDL--YQGETALHIAVVNQNLNLVRELIARGADVv 116

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1884823721 227 NAKCTDKM-------------TPLHYSASRGHVDIVTTLISHGASVNTLDSGDRTPL 270
Cdd:cd22192   117 SPRATGTFfrpgpknliyygeHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
Ank_4 pfam13637
Ankyrin repeats (many copies);
234-286 7.80e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.20  E-value: 7.80e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1884823721 234 MTPLHYSASRGHVDIVTTLISHGASVNTLDSGDRTPLKLAASRDLYQVVKVLV 286
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 205-285 3.01e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.36  E-value: 3.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 205 HLAAvRGHLDVVKCLLKMKAHVNAKCTDKMTPLHYSASRGHVDIVTTLISHGASVNTLDSGDRTPLKLAASRDLYQVVKV 284
Cdd:PTZ00322   88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                  .
gi 1884823721 285 L 285
Cdd:PTZ00322  167 L 167
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 129-272 3.77e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 53.33  E-value: 3.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 129 DLQWDTELEEISPVPDKVRQVEVDTGNSC-------SRVDAQ--DPRGRCALHYAAEAGQLEAVEYLIEAGSKVDLGDRE 199
Cdd:PLN03192  511 DLLGDNGGEHDDPNMASNLLTVASTGNAAlleellkAKLDPDigDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDAN 590

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 200 SLTPL-------H------------------------LAAVRGHLDVVKCLLKMKAHVNAKCTDKMTPLHYSASRGHVDI 248
Cdd:PLN03192  591 GNTALwnaisakHhkifrilyhfasisdphaagdllcTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDM 670

                         170       180
                  ....*....|....*....|....*..
gi 1884823721 249 VTTLISHGASV---NTLDsgDRTPLKL 272
Cdd:PLN03192  671 VRLLIMNGADVdkaNTDD--DFSPTEL 695
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 202-320 4.06e-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: 4.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 202 TPLHLAAVRGHLDVVKCLLKMKAHVNAKC-------TDKMTPLHYSASR-------GHVDIVTTLISHGASVNTLDSGDR 267
Cdd:TIGR00870 130 TALHLAAHRQNYEIVKLLLERGASVPARAcgdffvkSQGVDSFYHGESPlnaaaclGSPSIVALLSEDPADILTADSLGN 209

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1884823721 268 TPLKLAA------------SRDLYQ-VVKVLVESNAKVNIEDV---KGYTALCEAVWQKNVAMARLLLE 320
Cdd:TIGR00870 210 TLLHLLVmenefkaeyeelSCQMYNfALSLLDKLRDSKELEVIlnhQGLTPLKLAAKEGRIVLFRLKLA 278
Ank_5 pfam13857
Ankyrin repeats (many copies);
332-368 4.17e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.96  E-value: 4.17e-07
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1884823721 332 LHYAILHRHSEMIELLLEAGAMVNIRDDHGSTPLIVA 368
Cdd:pfam13857  20 LHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 171-382 7.27e-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: 52.32  E-value: 7.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 171 LHYAAEAGQLEAVEYLIEAGSkVDLGDRESL--TPLHLAAVRGHLDVVKCLLKMKAH-VNAKCTDKM----TPLHYSASR 243
Cdd:cd22192    21 LLLAAKENDVQAIKKLLKCPS-CDLFQRGALgeTALHVAALYDNLEAAVVLMEAAPElVNEPMTSDLyqgeTALHIAVVN 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 244 GHVDIVTTLISHGASVNT---------------LDSGDRtPLKLAASRDLYQVVKVLVESNAKVNIEDVKGYTALCEAVW 308
Cdd:cd22192   100 QNLNLVRELIARGADVVSpratgtffrpgpknlIYYGEH-PLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVL 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 309 QKNVAMArllleagakltptpfllhyailhrhSEMIELLLEAGAMVN------IRDDHGSTPLIVAAVTAQPTIIRLLLK 382
Cdd:cd22192   179 QPNKTFA-------------------------CQMYDLILSYDKEDDlqpldlVPNNQGLTPFKLAAKEGNIVMFQHLVQ 233
PHA03095 PHA03095
ankyrin-like protein; Provisional
 162-263 1.26e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 51.18  E-value: 1.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 162 AQDPRGRCALHYAAEAGQLEA--VEYLIEAGSKVDLGDRESLTPLHLAAVRGHLDVVKCLLKMKAHVNAKCTDKMTPLHY 239
Cdd:PHA03095  217 ATDMLGNTPLHSMATGSSCKRslVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSL 296

                          90       100
                  ....*....|....*....|....
gi 1884823721 240 SASRGHVDIVTTLISHGASVNTLD 263
Cdd:PHA03095  297 MVRNNNGRAVRAALAKNPSAETVA 320
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 125-264 1.82e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.05  E-value: 1.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 125 EGMADLQwdtelEEISPVPDKVRQVE------VDTGNSCSRVDAQDPrgrCALHY-AAEAGQLEA------VEYLIEAGS 191
Cdd:PTZ00322   35 ERMAAIQ-----EEIARIDTHLEALEatenkdATPDHNLTTEEVIDP---VVAHMlTVELCQLAAsgdavgARILLTGGA 106

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1884823721 192 KVDLGDRESLTPLHLAAVRGHLDVVKCLLKMKAHVNAKCTDKMTPLHYSASRGHVDIVTTLISHGASVNTLDS 264
Cdd:PTZ00322  107 DPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGA 179
PHA02798 PHA02798
ankyrin-like protein; Provisional
 180-383 2.17e-06

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 50.60  E-value: 2.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 180 LEAVEYLIEAGSKVDLGDRESLTPL-----HLAAVRGHLDVVKCLLKMKAHVNAKCTDKMTPLHYSASRGHV---DIVTT 251
Cdd:PHA02798   51 TDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYInnlEILLF 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 252 LISHGASVNTLDSGDRTPLK--LAASRDL-YQVVKVLVESNAKVNIEDVK-GYTALcEAVWQKNVA-----MARLLLEAG 322
Cdd:PHA02798  131 MIENGADTTLLDKDGFTMLQvyLQSNHHIdIEIIKLLLEKGVDINTHNNKeKYDTL-HCYFKYNIDridadILKLFVDNG 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 323 ------AKLTPTPFL-------------------------------------LHYAILHRHSEMIELLLEAGAMVNIRDD 359
Cdd:PHA02798  210 fiinkeNKSHKKKFMeylnsllydnkrfkknildfifsyidinqvdelgfnpLYYSVSHNNRKIFEYLLQLGGDINIITE 289

                         250       260
                  ....*....|....*....|....
gi 1884823721 360 HGSTPLIVAAVTAQPTIIRLLLKY 383
Cdd:PHA02798  290 LGNTCLFTAFENESKFIFNSILNK 313
PHA02798 PHA02798
ankyrin-like protein; Provisional
 213-457 2.32e-06

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 50.22  E-value: 2.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 213 LDVVKCLLKMKAHVNAKCTDKMTPL-----HYSASRGHVDIVTTLISHGASVNTLDSGDRTPLKLAASRDLY---QVVKV 284
Cdd:PHA02798   51 TDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYInnlEILLF 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 285 LVESNAKVNIEDVKGYTALCEAVWQKN---VAMARLLLEAGAKLTPTPFLLHYAILHRH---------SEMIELLLEAGA 352
Cdd:PHA02798  131 MIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINTHNNKEKYDTLHCYfkynidridADILKLFVDNGF 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 353 MVNIRDDHGSTPLIvaavtaqpTIIRLLLKYGAQVDfcgglswktpllsvlqtdhiptdlGVILELIMGGADV-DKACWD 431
Cdd:PHA02798  211 IINKENKSHKKKFM--------EYLNSLLYDNKRFK------------------------KNILDFIFSYIDInQVDELG 258

                         250       260
                  ....*....|....*....|....*.
gi 1884823721 432 MTPLYATICHNKVDAANLLLRHGASV 457
Cdd:PHA02798  259 FNPLYYSVSHNNRKIFEYLLQLGGDI 284
PHA02791 PHA02791
ankyrin-like protein; Provisional
 296-459 3.23e-06

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 49.27  E-value: 3.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 296 DVKGYTALCEAVWQKNVAMARLLLEAGA--KLTPTPFLLHYAILHRHSEMIELLLEAGAMVNIRDDHGSTPLIVAAVTAQ 373
Cdd:PHA02791   27 DVHGHSALYYAIADNNVRLVCTLLNAGAlkNLLENEFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGN 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 374 PTIIRLLLKYGAQVDFCGGLSWKTPLLSVLQTDhiptDLGVILELIMGGADVDKACWDMTPLYATICHNKVDAANLLLRH 453
Cdd:PHA02791  107 MQTVKLFVKKNWRLMFYGKTGWKTSFYHAVMLN----DVSIVSYFLSEIPSTFDLAILLSCIHITIKNGHVDMMILLLDY 182


                  ....*.
gi 1884823721 454 GASVTT 459
Cdd:PHA02791  183 MTSTNT 188
Ank_4 pfam13637
Ankyrin repeats (many copies);
331-381 3.30e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 3.30e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1884823721 331 LLHYAILHRHSEMIELLLEAGAMVNIRDDHGSTPLIVAAVTAQPTIIRLLL 381
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
226-273 3.44e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.26  E-value: 3.44e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1884823721 226 VNAKCTDKMTPLHYSASRGHVDIVTTLISHGASVNTLDSGDRTPLKLA 273
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 213-396 3.71e-06

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: 49.80  E-value: 3.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 213 LDVVKCLLKMKAHVNAKCTDK----MTPLHYSASRGHVDIVTTLISHGASVNTLDSGD--------------RTPLKLAA 274
Cdd:cd22196    70 LDIAEKTGNLKEFVNAAYTDSyykgQTALHIAIERRNMHLVELLVQNGADVHARASGEffkkkkggpgfyfgELPLSLAA 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 275 SRDLYQVVKVLVE---SNAKVNIEDVKGYTALCEAV-----WQKNVA----MARLLLEAGAKLTPTpfllhyailhrhse 342
Cdd:cd22196   150 CTNQLDIVKFLLEnphSPADISARDSMGNTVLHALVevadnTPENTKfvtkMYNEILILGAKIRPL-------------- 215

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1884823721 343 mieLLLEAgamvnIRDDHGSTPLIVAAVTAQPTIIRLLLKYGAQVDFCGGLSWK 396
Cdd:cd22196   216 ---LKLEE-----ITNKKGLTPLKLAAKTGKIGIFAYILGREIKEPECRHLSRK 261
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 198-365 4.08e-06

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 49.63  E-value: 4.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 198 RESLTPLHLAAVRGHLDVVKCLLKMK-AHVNAKCTDKMTPLHYSASRGHVDIVTTLIShgasvntldsGDRTPLKLAASR 276
Cdd:cd22192    15 RISESPLLLAAKENDVQAIKKLLKCPsCDLFQRGALGETALHVAALYDNLEAAVVLME----------AAPELVNEPMTS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 277 DLYQvvkvlvesnakvniedvkGYTALCEAVWQKNVAMARLLLEAGA-----KLTPTPFL-------------LHYAILH 338
Cdd:cd22192    85 DLYQ------------------GETALHIAVVNQNLNLVRELIARGAdvvspRATGTFFRpgpknliyygehpLSFAACV 146

                         170       180
                  ....*....|....*....|....*..
gi 1884823721 339 RHSEMIELLLEAGAMVNIRDDHGSTPL 365
Cdd:cd22192   147 GNEEIVRLLIEHGADIRAQDSLGNTVL 173
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 332-458 4.58e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 49.87  E-value: 4.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 332 LHYAILHRHSEMIELLLEAGAMVNIRDDHGSTPLIVAAVTAQPTIIRLLLKYGAQVD-FCGGlswktpllSVLQTDHIPT 410
Cdd:PLN03192  562 LHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDpHAAG--------DLLCTAAKRN 633

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1884823721 411 DLGVILELIMGGADVDKACWD-MTPLYATICHNKVDAANLLLRHGASVT 458
Cdd:PLN03192  634 DLTAMKELLKQGLNVDSEDHQgATALQVAMAEDHVDMVRLLIMNGADVD 682
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 202-382 7.40e-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: 48.72  E-value: 7.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 202 TPLHLAAVRGH----------LDVVKCLLKMKAHVNAKCTDKM----TPLHYSASRGHVDIVTTLISHGASVNTLDSGD- 266
Cdd:cd21882    28 TCLHKAALNLNdgvneaimllLEAAPDSGNPKELVNAPCTDEFyqgqTALHIAIENRNLNLVRLLVENGADVSARATGRf 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 267 ------------RTPLKLAASRDLYQVVKVLVESNAK---VNIEDVKGYTALCEAVWQKN---------VAMARLLLEAG 322
Cdd:cd21882   108 frkspgnlfyfgELPLSLAACTNQEEIVRLLLENGAQpaaLEAQDSLGNTVLHALVLQADntpensafvCQMYNLLLSYG 187

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 323 AKLTPTpfllhyailhrhsemieLLLEAgamvnIRDDHGSTPLIVAAVTAQPTIIRLLLK 382
Cdd:cd21882   188 AHLDPT-----------------QQLEE-----IPNHQGLTPLKLAAVEGKIVMFQHILQ 225
Ank_5 pfam13857
Ankyrin repeats (many copies);
186-239 8.15e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.49  E-value: 8.15e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1884823721 186 LIEAGSK-VDLGDRESLTPLHLAAVRGHLDVVKCLLKMKAHVNAKCTDKMTPLHY 239
Cdd:pfam13857   1 LLEHGPIdLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 180-373 8.49e-06

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 48.75  E-value: 8.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 180 LEAVEYLIEAGSKVDLGDRESLTPLHLAAVRGHL--DVVKCLLKMKAHVNAKCTDKMTP-LHYSASRGHVD--IVTTLIS 254
Cdd:PHA02716  192 IDILEWLCNNGVNVNLQNNHLITPLHTYLITGNVcaSVIKKIIELGGDMDMKCVNGMSPiMTYIINIDNINpeITNIYIE 271

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 255 H--GASVNTLDSGDRTPLKLAASRDLyQVVKVLVESNAKVNIEDVKGYTALCEAVWQKNVA--MARLLLEAGAKLT-PTP 329
Cdd:PHA02716  272 SldGNKVKNIPMILHSYITLARNIDI-SVVYSFLQPGVKLHYKDSAGRTCLHQYILRHNIStdIIKLLHEYGNDLNePDN 350

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1884823721 330 F---LLH-----YAILHRHS---------EMIELLLEAGAMVNIRDDHGSTPLIVAAVTAQ 373
Cdd:PHA02716  351 IgntVLHtylsmLSVVNILDpetdndirlDVIQCLISLGADITAVNCLGYTPLTSYICTAQ 411
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 232-260 1.26e-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: 1.26e-05
                           10        20
                   ....*....|....*....|....*....
gi 1884823721  232 DKMTPLHYSASRGHVDIVTTLISHGASVN 260
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank_5 pfam13857
Ankyrin repeats (many copies);
159-207 1.57e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.72  E-value: 1.57e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1884823721 159 RVDAQDPRGRCALHYAAEAGQLEAVEYLIEAGSKVDLGDRESLTPLHLA 207
Cdd:pfam13857   8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 160-231 1.60e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 47.35  E-value: 1.60e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1884823721 160 VDAQDPRGRCALHYAAEAGQLEAVEYLIEAGSKVDLGDRESLTPLHLAAVRGHLDVVKCLLKMKAHVNAKCT 231
Cdd:PHA03100  185 INIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 213-382 2.55e-05

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: 47.10  E-value: 2.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 213 LDVVKCLLKMKAHVNAKCTDK----MTPLHYSASRGHVDIVTTLISHGASVNTLDSGD--------------RTPLKLAA 274
Cdd:cd22193    52 LDIAEKTDNLKRFINAEYTDEyyegQTALHIAIERRQGDIVALLVENGADVHAHAKGRffqpkyqgegfyfgELPLSLAA 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 275 SRDLYQVVKVLVES---NAKVNIEDVKGYTALCEAV-----WQKNVA----MARLLLEAGAKLTPTpfllhyailhrhse 342
Cdd:cd22193   132 CTNQPDIVQYLLENehqPADIEAQDSRGNTVLHALVtvadnTKENTKfvtrMYDMILIRGAKLCPT-------------- 197

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1884823721 343 mieLLLEAgamvnIRDDHGSTPLIVAAVTAQPTIIRLLLK 382
Cdd:cd22193   198 ---VELEE-----IRNNDGLTPLQLAAKMGKIEILKYILQ 229
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 202-229 4.16e-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: 40.74  E-value: 4.16e-05
                          10        20
                  ....*....|....*....|....*....
gi 1884823721 202 TPLHLAAVR-GHLDVVKCLLKMKAHVNAK 229
Cdd:pfam00023   4 TPLHLAAGRrGNLEIVKLLLSKGADVNAR 32
Ank_2 pfam12796
Ankyrin repeats (3 copies);
159-197 4.49e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 42.41  E-value: 4.49e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1884823721 159 RVDAQDpRGRCALHYAAEAGQLEAVEYLIEAGSKVDLGD 197
Cdd:pfam12796  54 DVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 202-228 5.06e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 40.26  E-value: 5.06e-05
                           10        20
                   ....*....|....*....|....*..
gi 1884823721  202 TPLHLAAVRGHLDVVKCLLKMKAHVNA 228
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 303-392 5.71e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.04  E-value: 5.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 303 LCEAVWQKNVAMARLLLEAGAKLTPTPF----LLHYAILHRHSEMIELLLEAGAMVNIRDDHGSTPLIVAAVTAQPTIIR 378
Cdd:PTZ00322   86 LCQLAASGDAVGARILLTGGADPNCRDYdgrtPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165

                          90
                  ....*....|....
gi 1884823721 379 LLLKYgAQVDFCGG 392
Cdd:PTZ00322  166 LLSRH-SQCHFELG 178
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 232-263 5.98e-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: 5.98e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1884823721 232 DKMTPLHYSASR-GHVDIVTTLISHGASVNTLD 263
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 332-381 9.49e-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: 45.52  E-value: 9.49e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1884823721 332 LHYAILHRHSEMIELLLEAGAMVNI-----------RDD---HGSTPLIVAAVTAQPTIIRLLL 381
Cdd:cd22194   145 LNIAIERRQGDIVKLLIAKGADVNAhakgvffnpkyKHEgfyFGETPLALAACTNQPEIVQLLM 208
Ank_4 pfam13637
Ankyrin repeats (many copies);
267-319 1.26e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.95  E-value: 1.26e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1884823721 267 RTPLKLAASRDLYQVVKVLVESNAKVNIEDVKGYTALCEAVWQKNVAMARLLL 319
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 202-228 4.85e-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: 37.62  E-value: 4.85e-04
                          10        20
                  ....*....|....*....|....*..
gi 1884823721 202 TPLHLAAVRGHLDVVKCLLKMKAHVNA 228
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADINA 30
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
 523-562 7.00e-04

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


Pssm-ID: 462192  Cd Length: 39  Bit Score: 37.53  E-value: 7.00e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1884823721 523 PLKLSELARIKIRSLWPRRCSmaDYVRSLGLPRLLEEYLL 562
Cdd:pfam07525   2 PRSLQHLCRLAIRRALGKRRL--GAIDKLPLPPLLKDYLL 39
Ank_5 pfam13857
Ankyrin repeats (many copies);
252-303 9.32e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.71  E-value: 9.32e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1884823721 252 LISHG-ASVNTLDSGDRTPLKLAASRDLYQVVKVLVESNAKVNIEDVKGYTAL 303
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 268-385 9.37e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 42.31  E-value: 9.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 268 TPLKLAASRDLYQVVKVLVESN-AKVNIEDVKGYTALCEAVWQKNVAMARLLLEAGAKL-----TPTPFL----LHYAIL 337
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPsCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELvnepmTSDLYQgetaLHIAVV 98

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1884823721 338 HRHSEMIELLLEAGA-MVNIRDD-------------HGSTPLIVAAVTAQPTIIRLLLKYGA 385
Cdd:cd22192    99 NQNLNLVRELIARGAdVVSPRATgtffrpgpknliyYGEHPLSFAACVGNEEIVRLLIEHGA 160
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 328-359 1.30e-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: 1.30e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1884823721 328 TPflLHYAILHR-HSEMIELLLEAGAMVNIRDD 359
Cdd:pfam00023   4 TP--LHLAAGRRgNLEIVKLLLSKGADVNARDK 34
SOCS cd03587
SOCS (suppressors of cytokine signaling) box. The SOCS box is found in the C-terminal region ...
 523-562 2.05e-03

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


Pssm-ID: 239641  Cd Length: 41  Bit Score: 36.29  E-value: 2.05e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1884823721 523 PLKLSELARIKIRSLWPRRCsmADYVRSLGLPRLLEEYLL 562
Cdd:cd03587     2 PRSLQHLCRLAIRRCLGKRR--LDLIDKLPLPPRLKDYLL 39
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 299-387 2.09e-03

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 41.02  E-value: 2.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 299 GYTALCEAVWQKN---VAMARLLLEAGAKL-TPTPFL--------------LHYAILHRHSEMIELLLEAGAMVNIRDD- 359
Cdd:cd21882    26 GKTCLHKAALNLNdgvNEAIMLLLEAAPDSgNPKELVnapctdefyqgqtaLHIAIENRNLNLVRLLVENGADVSARATg 105

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1884823721 360 ------------HGSTPLIVAAVTAQPTIIRLLLKYGAQV 387
Cdd:cd21882   106 rffrkspgnlfyFGELPLSLAACTNQEEIVRLLLENGAQP 145
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 162-276 2.20e-03

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 40.90  E-value: 2.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 162 AQDPRGRCALHYAAEAGQLEAVEYLIEAGSKVDLGDRESL--------------TPLHLAAVRGHLDVVKCLLKmKAHVN 227
Cdd:cd22194   136 EEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVFfnpkykhegfyfgeTPLALAACTNQPEIVQLLME-KESTD 214

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1884823721 228 AKCTDKM--TPLH-----YSASRGHVDIVTTLI------SHGASVNTLDSGDR-TPLKLAASR 276
Cdd:cd22194   215 ITSQDSRgnTVLHalvtvAEDSKTQNDFVKRMYdmillkSENKNLETIRNNEGlTPLQLAAKM 277
PHA02946 PHA02946
ankyin-like protein; Provisional
 232-381 2.51e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 40.42  E-value: 2.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 232 DKMTPLHYSASRGHVDIVTTLISHGASVNTLDSGDRTPLKLAASRD--LYQVVKVLVESNAKVNIE-DVKGYTAL----- 303
Cdd:PHA02946   71 DGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDdeVIERINLLVQYGAKINNSvDEEGCGPLlactd 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 304 -CEAVWQKNVAM---ARLLLEAGAKltptpfllHyaiLHRH-------SEMIELLLEAGAMVNIRDDHGSTPL-IVAAVT 371
Cdd:PHA02946  151 pSERVFKKIMSIgfeARIVDKFGKN--------H---IHRHlmsdnpkASTISWMMKLGISPSKPDHDGNTPLhIVCSKT 219

                         170
                  ....*....|.
gi 1884823721 372 AQPT-IIRLLL 381
Cdd:PHA02946  220 VKNVdIINLLL 230
PHA02798 PHA02798
ankyrin-like protein; Provisional
 337-459 2.99e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 40.59  E-value: 2.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 337 LHRHS---EMIELLLEAGAMVNIRDDHGSTPL--IVAAVTAQPT---IIRLLLKYGAQVDfCGGLSWKTPLLSVLQTDHI 408
Cdd:PHA02798   44 LQRDSpstDIVKLFINLGANVNGLDNEYSTPLctILSNIKDYKHmldIVKILIENGADIN-KKNSDGETPLYCLLSNGYI 122

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1884823721 409 pTDLGVILELIMGGADV---DKACWDMTPLY-ATICHNKVDAANLLLRHGASVTT 459
Cdd:PHA02798  123 -NNLEILLFMIENGADTtllDKDGFTMLQVYlQSNHHIDIEIIKLLLEKGVDINT 176
PHA02946 PHA02946
ankyin-like protein; Provisional
 293-406 3.20e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 40.42  E-value: 3.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 293 NIEDVKGYTALCEAVWQKNVAMARLLLEAgakLTPTPfllHYAILHRH-------SEMIELLLEAGAMVNIRDDHGSTPL 365
Cdd:PHA02946    3 NIMSAEYYLSLYAKYNSKNLDVFRNMLQA---IEPSG---NYHILHAYcgikgldERFVEELLHRGYSPNETDDDGNYPL 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1884823721 366 IVAAVTAQPTIIRLLLKYGAQVDFCGGLSwKTPLLSVLQTD 406
Cdd:PHA02946   77 HIASKINNNRIVAMLLTHGADPNACDKQH-KTPLYYLSGTD 116
Ank_4 pfam13637
Ankyrin repeats (many copies);
299-348 3.29e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.10  E-value: 3.29e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1884823721 299 GYTALCEAVWQKNVAMARLLLEAGAKLTPTPF----LLHYAILHRHSEMIELLL 348
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGngetALHFAASNGNVEVLKLLL 54
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 234-459 4.30e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 39.72  E-value: 4.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 234 MTPLH-YSASRGHVDI--VTTLISHGASVNTLDSGDRTPLKLAASRDLY-QVVKVLVESNAKVNiedVKGY--TALCEav 307
Cdd:PHA02989    1 MSSLYeYILYSDTVDKnaLEFLLRTGFDVNEEYRGNSILLLYLKRKDVKiKIVKLLIDNGADVN---YKGYieTPLCA-- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 308 wqknvamarllleagakltptpFLLHYAIL-HRHSEMIELLLEAGAMVNIRDDHGSTPL---IVAAVTAQPTIIRLLLKY 383
Cdd:PHA02989   76 ----------------------VLRNREITsNKIKKIVKLLLKFGADINLKTFNGVSPIvcfIYNSNINNCDMLRFLLSK 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 384 GAQVDFCGGLSWKTPLLSVLQTDHIPTDlgVILELIMGGADV--DKACWDMTP----LYATICHNKVDAANLLLRHGASV 457
Cdd:PHA02989  134 GINVNDVKNSRGYNLLHMYLESFSVKKD--VIKILLSFGVNLfeKTSLYGLTPmniyLRNDIDVISIKVIKYLIKKGVNI 211


                  ..
gi 1884823721 458 TT 459
Cdd:PHA02989  212 ET 213
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 166-198 4.80e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.96  E-value: 4.80e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1884823721 166 RGRCALHYAA-EAGQLEAVEYLIEAGSKVDLGDR 198
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 328-356 5.49e-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: 5.49e-03
                           10        20
                   ....*....|....*....|....*....
gi 1884823721  328 TPflLHYAILHRHSEMIELLLEAGAMVNI 356
Cdd:smart00248   4 TP--LHLAAENGNLEVVKLLLDKGADINA 30
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 335-455 5.85e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 39.20  E-value: 5.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 335 AILHRHSEMIELLLEAGAMVNIRDDHGSTPLIVAAVTAQPTIIRLLLKYGAQVDFcgglswKTP-LLSVLQTDHIPTDLG 413
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDV------KYPdIESELHDAVEEGDVK 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1884823721 414 VILELIMGGADVDKACWD--MTPLYATICHNKVDAANLLLRHGA 455
Cdd:PHA02875   83 AVEELLDLGKFADDVFYKdgMTPLHLATILKKLDIMKLLIARGA 126
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 166-194 6.19e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.54  E-value: 6.19e-03
                          10        20
                  ....*....|....*....|....*....
gi 1884823721 166 RGRCALHYAAEAGQLEAVEYLIEAGSKVD 194
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 232-261 6.31e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.54  E-value: 6.31e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1884823721 232 DKMTPLHYSASRGHVDIVTTLISHGASVNT 261
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
SOCS_ASB3 cd03722
SOCS (suppressors of cytokine signaling) box of ASB3-like proteins. ASB family members have a ...
 526-566 6.75e-03

SOCS (suppressors of cytokine signaling) box of ASB3-like proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. ABS3 has been shown to be negative regulator of TNF-R2-mediated cellular responses to TNF-alpha by direct targeting of tumor necrosis factor receptor II (TNF-R2) for ubiquitination and proteasome-mediated degradation. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


Pssm-ID: 239692  Cd Length: 51  Bit Score: 35.15  E-value: 6.75e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1884823721 526 LSELARIKIRS-LWPRRCSMADYVRSLGLPRLLEEYLLISEI 566
Cdd:cd03722     6 LTHLCRLEIRSsLKSERLRSDSFICQLPLPRSLQDYLLYSDV 47
PHA02791 PHA02791
ankyrin-like protein; Provisional
 235-325 7.05e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 38.87  E-value: 7.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 235 TPLHYSASRGHVDIVTTLISHGASVNTLDsgDRTPLKLAASRDLYQVVKVLVESNAKVNIEDVKGYTALCEAVWQKNVAM 314
Cdd:PHA02791   32 SALYYAIADNNVRLVCTLLNAGALKNLLE--NEFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGNMQT 109

                          90
                  ....*....|.
gi 1884823721 315 ARLLLEAGAKL 325
Cdd:PHA02791  110 VKLFVKKNWRL 120
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 238-330 7.98e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 39.11  E-value: 7.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884823721 238 HYSASRGHVDIvTTLISHGASVNTLDSGDRTPLKLAASRDLYQVVKVLVESNAKVNIEDVKGYTALCEAVWQKNVAMARL 317
Cdd:PTZ00322   88 QLAASGDAVGA-RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166

                          90       100
                  ....*....|....*....|
gi 1884823721 318 LL-------EAGAKLTPTPF 330
Cdd:PTZ00322  167 LSrhsqchfELGANAKPDSF 186
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 170-195 9.52e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.10  E-value: 9.52e-03
                           10        20
                   ....*....|....*....|....*.
gi 1884823721  170 ALHYAAEAGQLEAVEYLIEAGSKVDL 195
Cdd:smart00248   5 PLHLAAENGNLEVVKLLLDKGADINA 30
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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