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Conserved domains on  [gi|240255309|ref|NP_187566|]
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Ankyrin repeat family protein [Arabidopsis thaliana]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 12122272)

ankyrin repeat (ANK) domain-containing protein may be involved in mediating protein-protein interactions

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PGG pfam13962
Domain of unknown function; The PGG domain is named for the highly conserved sequence motif ...
428-533 3.94e-36

Domain of unknown function; The PGG domain is named for the highly conserved sequence motif found at the startt of the domain. The function is not known.


:

Pssm-ID: 433609  Cd Length: 114  Bit Score: 131.14  E-value: 3.94e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309  428 GINNATNSVTVVAVLFATVAFAAIFTVPGG---DDDH---GVAVMVHATSFKIFFIFNAIALFTSLAVVVVQITLVRGET 501
Cdd:pfam13962   3 WLKEARNTLLLVATLIATVTFAAGFTPPGGywqDDDGphaGKPILAKNPAFKAFVISNAIAFFASLVAVVLLLSIVSDFL 82
                          90       100       110
                  ....*....|....*....|....*....|..
gi 240255309  502 KTERRVVEVINKLMWLASVCTTVAFISSSYIV 533
Cdd:pfam13962  83 RSLPRKLRIGLKLLWVALLSMLVAFAAGSYRV 114
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
91-383 3.07e-30

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 120.44  E-value: 3.07e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309  91 ELHLAAQRGDLASVKQILSDIDSQITGTITGADFDDEVAQIMTSVVNEVNELGETPLFTAAEKGNIDVVKELLPYttIES 170
Cdd:COG0666    2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAA--GAD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 171 LMQKNLSGFDALHIACSQGHRSIVQLLLEHEPQLsKTVAQSNATPLVSAATRGHSEVVNELLAKDSSLlEISRSNGKNAL 250
Cdd:COG0666   80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGADV-NARDKDGETPLHLAAYNGNLEIVKLLLEAGADV-NAQDNDGNTPL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 251 HLAARQGHVDIVRTLLDKDPQLARRtDKKGQTSLHMAVKGVSSQVVRLLLRADpAIVMLPDKFGNTVLHIATRKKRAEIV 330
Cdd:COG0666  158 HLAAANGNLEIVKLLLEAGADVNAR-DNDGETPLHLAAENGHLEIVKLLLEAG-ADVNAKDNDGKTALDLAAENGNLEIV 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 240255309 331 NELLQLPDtNVNALTRDHKTAYDIAEGLTHSEETAEIKEILSRCGALKANELN 383
Cdd:COG0666  236 KLLLEAGA-DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
NAM-associated super family cl24049
No apical meristem-associated C-terminal domain; This domain is found in a number of different ...
20-107 6.85e-03

No apical meristem-associated C-terminal domain; This domain is found in a number of different types of plant proteins including NAM-like proteins.


The actual alignment was detected with superfamily member pfam14303:

Pssm-ID: 464129  Cd Length: 142  Bit Score: 37.46  E-value: 6.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309   20 ATDPTSPTGSTVADLSPTPTPRKTLVLSNSGKALMVSNSSKSLGLSNSGKRfdPTGKKKY---VKQVTGRHNDTELHLAA 96
Cdd:pfam14303  27 NKKPSSTASSSPAPTSLASTDPDTDSSDSSSAGSNESNSDDSSPSSKSPTR--PIGRKKAkekRQEELDAAKEEKKQNDI 104
                          90
                  ....*....|.
gi 240255309   97 QRGDLASVKQI 107
Cdd:pfam14303 105 EEAQVAAELRL 115
 
Name Accession Description Interval E-value
PGG pfam13962
Domain of unknown function; The PGG domain is named for the highly conserved sequence motif ...
428-533 3.94e-36

Domain of unknown function; The PGG domain is named for the highly conserved sequence motif found at the startt of the domain. The function is not known.


Pssm-ID: 433609  Cd Length: 114  Bit Score: 131.14  E-value: 3.94e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309  428 GINNATNSVTVVAVLFATVAFAAIFTVPGG---DDDH---GVAVMVHATSFKIFFIFNAIALFTSLAVVVVQITLVRGET 501
Cdd:pfam13962   3 WLKEARNTLLLVATLIATVTFAAGFTPPGGywqDDDGphaGKPILAKNPAFKAFVISNAIAFFASLVAVVLLLSIVSDFL 82
                          90       100       110
                  ....*....|....*....|....*....|..
gi 240255309  502 KTERRVVEVINKLMWLASVCTTVAFISSSYIV 533
Cdd:pfam13962  83 RSLPRKLRIGLKLLWVALLSMLVAFAAGSYRV 114
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
91-383 3.07e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 120.44  E-value: 3.07e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309  91 ELHLAAQRGDLASVKQILSDIDSQITGTITGADFDDEVAQIMTSVVNEVNELGETPLFTAAEKGNIDVVKELLPYttIES 170
Cdd:COG0666    2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAA--GAD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 171 LMQKNLSGFDALHIACSQGHRSIVQLLLEHEPQLsKTVAQSNATPLVSAATRGHSEVVNELLAKDSSLlEISRSNGKNAL 250
Cdd:COG0666   80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGADV-NARDKDGETPLHLAAYNGNLEIVKLLLEAGADV-NAQDNDGNTPL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 251 HLAARQGHVDIVRTLLDKDPQLARRtDKKGQTSLHMAVKGVSSQVVRLLLRADpAIVMLPDKFGNTVLHIATRKKRAEIV 330
Cdd:COG0666  158 HLAAANGNLEIVKLLLEAGADVNAR-DNDGETPLHLAAENGHLEIVKLLLEAG-ADVNAKDNDGKTALDLAAENGNLEIV 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 240255309 331 NELLQLPDtNVNALTRDHKTAYDIAEGLTHSEETAEIKEILSRCGALKANELN 383
Cdd:COG0666  236 KLLLEAGA-DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
Ank_2 pfam12796
Ankyrin repeats (3 copies);
182-269 8.21e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.92  E-value: 8.21e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309  182 LHIACSQGHRSIVQLLLEHEPQLsKTVAQSNATPLVSAATRGHSEVVNELLAKDSSLLeisRSNGKNALHLAARQGHVDI 261
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADA-NLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL---KDNGRTALHYAARSGHLEI 76

                  ....*...
gi 240255309  262 VRTLLDKD 269
Cdd:pfam12796  77 VKLLLEKG 84
PHA03100 PHA03100
ankyrin repeat protein; Provisional
145-335 3.42e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 81.25  E-value: 3.42e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 145 TPLFTAAEKGNIDVVKELLpYTTIeSLMQKNLSGFDALHIACSQGH-----RSIVQLLLEHEPQLSKTVAQSNaTPLVSA 219
Cdd:PHA03100  37 LPLYLAKEARNIDVVKILL-DNGA-DINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGI-TPLLYA 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 220 ATR--GHSEVVNELLAKDSSLlEISRSNGKNALHLAARQGHVD--IVRTLLDK--DPQLARR-------------TDKKG 280
Cdd:PHA03100 114 ISKksNSYSIVEYLLDNGANV-NIKNSDGENLLHLYLESNKIDlkILKLLIDKgvDINAKNRvnyllsygvpiniKDVYG 192
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 240255309 281 QTSLHMAVKGVSSQVVRLLLR--ADPAIVmlpDKFGNTVLHIATRKKRAEIVNELLQ 335
Cdd:PHA03100 193 FTPLHYAVYNNNPEFVKYLLDlgANPNLV---NKYGDTPLHIAILNNNKEIFKLLLN 246
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
144-359 1.54e-12

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: 70.43  E-value: 1.54e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 144 ETPLFTAAEKGNIDVVKELLPYTTIEsLMQKNLSGFDALHIACSQGHRSIVQLLLEHEPQLsktvaqsnatplvsaatrg 223
Cdd:cd22192   18 ESPLLLAAKENDVQAIKKLLKCPSCD-LFQRGALGETALHVAALYDNLEAAVVLMEAAPEL------------------- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 224 hsevVNEllAKDSSLLEisrsnGKNALHLAARQGHVDIVRTLLDK--DPQLARRTD---KKGQTSL-----HM----AVK 289
Cdd:cd22192   78 ----VNE--PMTSDLYQ-----GETALHIAVVNQNLNLVRELIARgaDVVSPRATGtffRPGPKNLiyygeHPlsfaACV 146
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 240255309 290 GvSSQVVRLLLRADPAIVMlPDKFGNTVLHI----ATRKKRAEIVNELLQLpDTNVNALTRDHKTAYDiaeGLT 359
Cdd:cd22192  147 G-NEEIVRLLIEHGADIRA-QDSLGNTVLHIlvlqPNKTFACQMYDLILSY-DKEDDLQPLDLVPNNQ---GLT 214
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
95-321 6.01e-10

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 62.41  E-value: 6.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309   95 AAQRGDLASVKQILsdidsqitgtitgadfddevAQIMTSVVNEVNELGETPLFTAAEKGNIDVVKELLPYTTIESLMQK 174
Cdd:TIGR00870  24 AAERGDLASVYRDL--------------------EEPKKLNINCPDRLGRSALFVAAIENENLELTELLLNLSCRGAVGD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309  175 NLsgfdaLHIAcSQGHRSIVQLLLEHEPQLsktvaqsnatplvsaatrgHSEVVNELLAKDSSLLEISRsnGKNALHLAA 254
Cdd:TIGR00870  84 TL-----LHAI-SLEYVDAVEAILLHLLAA-------------------FRKSGPLELANDQYTSEFTP--GITALHLAA 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309  255 RQGHVDIVRTLLDKDPQLARR------TDKKGQTSLHM------AVKGVSS-QVVRLLLRaDPAIVMLPDKFGNTVLHIA 321
Cdd:TIGR00870 137 HRQNYEIVKLLLERGASVPARacgdffVKSQGVDSFYHgesplnAAACLGSpSIVALLSE-DPADILTADSLGNTLLHLL 215
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
245-270 1.71e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.11  E-value: 1.71e-04
                           10        20
                   ....*....|....*....|....*.
gi 240255309   245 NGKNALHLAARQGHVDIVRTLLDKDP 270
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
NAM-associated pfam14303
No apical meristem-associated C-terminal domain; This domain is found in a number of different ...
20-107 6.85e-03

No apical meristem-associated C-terminal domain; This domain is found in a number of different types of plant proteins including NAM-like proteins.


Pssm-ID: 464129  Cd Length: 142  Bit Score: 37.46  E-value: 6.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309   20 ATDPTSPTGSTVADLSPTPTPRKTLVLSNSGKALMVSNSSKSLGLSNSGKRfdPTGKKKY---VKQVTGRHNDTELHLAA 96
Cdd:pfam14303  27 NKKPSSTASSSPAPTSLASTDPDTDSSDSSSAGSNESNSDDSSPSSKSPTR--PIGRKKAkekRQEELDAAKEEKKQNDI 104
                          90
                  ....*....|.
gi 240255309   97 QRGDLASVKQI 107
Cdd:pfam14303 105 EEAQVAAELRL 115
 
Name Accession Description Interval E-value
PGG pfam13962
Domain of unknown function; The PGG domain is named for the highly conserved sequence motif ...
428-533 3.94e-36

Domain of unknown function; The PGG domain is named for the highly conserved sequence motif found at the startt of the domain. The function is not known.


Pssm-ID: 433609  Cd Length: 114  Bit Score: 131.14  E-value: 3.94e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309  428 GINNATNSVTVVAVLFATVAFAAIFTVPGG---DDDH---GVAVMVHATSFKIFFIFNAIALFTSLAVVVVQITLVRGET 501
Cdd:pfam13962   3 WLKEARNTLLLVATLIATVTFAAGFTPPGGywqDDDGphaGKPILAKNPAFKAFVISNAIAFFASLVAVVLLLSIVSDFL 82
                          90       100       110
                  ....*....|....*....|....*....|..
gi 240255309  502 KTERRVVEVINKLMWLASVCTTVAFISSSYIV 533
Cdd:pfam13962  83 RSLPRKLRIGLKLLWVALLSMLVAFAAGSYRV 114
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
91-383 3.07e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 120.44  E-value: 3.07e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309  91 ELHLAAQRGDLASVKQILSDIDSQITGTITGADFDDEVAQIMTSVVNEVNELGETPLFTAAEKGNIDVVKELLPYttIES 170
Cdd:COG0666    2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAA--GAD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 171 LMQKNLSGFDALHIACSQGHRSIVQLLLEHEPQLsKTVAQSNATPLVSAATRGHSEVVNELLAKDSSLlEISRSNGKNAL 250
Cdd:COG0666   80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGADV-NARDKDGETPLHLAAYNGNLEIVKLLLEAGADV-NAQDNDGNTPL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 251 HLAARQGHVDIVRTLLDKDPQLARRtDKKGQTSLHMAVKGVSSQVVRLLLRADpAIVMLPDKFGNTVLHIATRKKRAEIV 330
Cdd:COG0666  158 HLAAANGNLEIVKLLLEAGADVNAR-DNDGETPLHLAAENGHLEIVKLLLEAG-ADVNAKDNDGKTALDLAAENGNLEIV 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 240255309 331 NELLQLPDtNVNALTRDHKTAYDIAEGLTHSEETAEIKEILSRCGALKANELN 383
Cdd:COG0666  236 KLLLEAGA-DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
136-351 2.24e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 115.05  E-value: 2.24e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 136 VNEVNELGETPLFTAAEKGNIDVVKELLPYttIESLMQKNLSGFDALHIACSQGHRSIVQLLLEHEPQLSKTVAQSNaTP 215
Cdd:COG0666   80 INAKDDGGNTLLHAAARNGDLEIVKLLLEA--GADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGN-TP 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 216 LVSAATRGHSEVVNELLAKDSSLlEISRSNGKNALHLAARQGHVDIVRTLLDK--DPQLarrTDKKGQTSLHMAVKGVSS 293
Cdd:COG0666  157 LHLAAANGNLEIVKLLLEAGADV-NARDNDGETPLHLAAENGHLEIVKLLLEAgaDVNA---KDNDGKTALDLAAENGNL 232
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 240255309 294 QVVRLLLRADpAIVMLPDKFGNTVLHIATRKKRAEIVNELLQLPDTNVNALTRDHKTA 351
Cdd:COG0666  233 EIVKLLLEAG-ADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
168-421 1.91e-25

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 106.58  E-value: 1.91e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 168 IESLMQKNLSGFDALHIACSQGHRSIVQLLLEHEPQLSKTVAQSNATPLVSAATRGHSEVVNELLAKDSSLlEISRSNGK 247
Cdd:COG0666   43 ALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADV-NARDKDGE 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 248 NALHLAARQGHVDIVRTLLDK--DPQLarrTDKKGQTSLHMAVKGVSSQVVRLLLRADpAIVMLPDKFGNTVLHIATRKK 325
Cdd:COG0666  122 TPLHLAAYNGNLEIVKLLLEAgaDVNA---QDNDGNTPLHLAAANGNLEIVKLLLEAG-ADVNARDNDGETPLHLAAENG 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 326 RAEIVNELLQLpDTNVNALTRDHKTAYDIAEGLTHseetAEIKEILSRCGALKANELNQPRDELRKTVTEIKKDVHTQLE 405
Cdd:COG0666  198 HLEIVKLLLEA-GADVNAKDNDGKTALDLAAENGN----LEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLL 272
                        250
                 ....*....|....*.
gi 240255309 406 QTRKTNKNVDGIAKEL 421
Cdd:COG0666  273 LALLLLAAALLDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
76-316 2.39e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 103.50  E-value: 2.39e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309  76 KKKYVKQVTGRHNDTELHLAAQRGDLASVKQILSDidsqitgtitGADfddevaqimtsvVNEVNELGETPLFTAAEKGN 155
Cdd:COG0666   75 AAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA----------GAD------------VNARDKDGETPLHLAAYNGN 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 156 IDVVKELL-----PYttieslmQKNLSGFDALHIACSQGHRSIVQLLLEHEPQLsKTVAQSNATPLVSAATRGHSEVVNE 230
Cdd:COG0666  133 LEIVKLLLeagadVN-------AQDNDGNTPLHLAAANGNLEIVKLLLEAGADV-NARDNDGETPLHLAAENGHLEIVKL 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 231 LLAKDSSlLEISRSNGKNALHLAARQGHVDIVRTLLDKDPQLARRtDKKGQTSLHMAVKGVSSQVVRLLLRADPAIVMLP 310
Cdd:COG0666  205 LLEAGAD-VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAK-DKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282

                 ....*.
gi 240255309 311 DKFGNT 316
Cdd:COG0666  283 LDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
159-355 2.80e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 85.78  E-value: 2.80e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 159 VKELLPYTTIESLMQKNLSGFDALHIACSQGHRSIVQLLLEHEPQLSKTVAQSNATPLVSAATRGHSEVVNELLAKDSsL 238
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGA-D 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 239 LEISRSNGKNALHLAARQGHVDIVRTLLDKDPQLARRtDKKGQTSLHMAVKGVSSQVVRLLLRADpAIVMLPDKFGNTVL 318
Cdd:COG0666   80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNAR-DKDGETPLHLAAYNGNLEIVKLLLEAG-ADVNAQDNDGNTPL 157
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 240255309 319 HIATRKKRAEIVNELLQLpDTNVNALTRDHKTAYDIA 355
Cdd:COG0666  158 HLAAANGNLEIVKLLLEA-GADVNARDNDGETPLHLA 193
Ank_2 pfam12796
Ankyrin repeats (3 copies);
182-269 8.21e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.92  E-value: 8.21e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309  182 LHIACSQGHRSIVQLLLEHEPQLsKTVAQSNATPLVSAATRGHSEVVNELLAKDSSLLeisRSNGKNALHLAARQGHVDI 261
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADA-NLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL---KDNGRTALHYAARSGHLEI 76

                  ....*...
gi 240255309  262 VRTLLDKD 269
Cdd:pfam12796  77 VKLLLEKG 84
PHA03100 PHA03100
ankyrin repeat protein; Provisional
145-335 3.42e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 81.25  E-value: 3.42e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 145 TPLFTAAEKGNIDVVKELLpYTTIeSLMQKNLSGFDALHIACSQGH-----RSIVQLLLEHEPQLSKTVAQSNaTPLVSA 219
Cdd:PHA03100  37 LPLYLAKEARNIDVVKILL-DNGA-DINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGI-TPLLYA 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 220 ATR--GHSEVVNELLAKDSSLlEISRSNGKNALHLAARQGHVD--IVRTLLDK--DPQLARR-------------TDKKG 280
Cdd:PHA03100 114 ISKksNSYSIVEYLLDNGANV-NIKNSDGENLLHLYLESNKIDlkILKLLIDKgvDINAKNRvnyllsygvpiniKDVYG 192
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 240255309 281 QTSLHMAVKGVSSQVVRLLLR--ADPAIVmlpDKFGNTVLHIATRKKRAEIVNELLQ 335
Cdd:PHA03100 193 FTPLHYAVYNNNPEFVKYLLDlgANPNLV---NKYGDTPLHIAILNNNKEIFKLLLN 246
Ank_2 pfam12796
Ankyrin repeats (3 copies);
92-207 4.17e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 73.61  E-value: 4.17e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309   92 LHLAAQRGDLASVKQILSdidsqitgtiTGADfddevaqimtsvVNEVNELGETPLFTAAEKGNIDVVKELLPYTTIESl 171
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLE----------NGAD------------ANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL- 57
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 240255309  172 mqkNLSGFDALHIACSQGHRSIVQLLLEHEPQLSKT 207
Cdd:pfam12796  58 ---KDNGRTALHYAARSGHLEIVKLLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
147-238 1.79e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.99  E-value: 1.79e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309  147 LFTAAEKGNIDVVKELLPYttIESLMQKNLSGFDALHIACSQGHRSIVQLLLEHEPQLSKTvaqSNATPLVSAATRGHSE 226
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLEN--GADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD---NGRTALHYAARSGHLE 75
                          90
                  ....*....|..
gi 240255309  227 VVNELLAKDSSL 238
Cdd:pfam12796  76 IVKLLLEKGADI 87
Ank_2 pfam12796
Ankyrin repeats (3 copies);
250-335 5.11e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.14  E-value: 5.11e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309  250 LHLAARQGHVDIVRTLLDKDPQlARRTDKKGQTSLHMAVKGVSSQVVRLLLRAdpAIVMLPDKfGNTVLHIATRKKRAEI 329
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGAD-ANLQDKNGRTALHLAAKNGHLEIVKLLLEH--ADVNLKDN-GRTALHYAARSGHLEI 76

                  ....*.
gi 240255309  330 VNELLQ 335
Cdd:pfam12796  77 VKLLLE 82
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
144-359 1.54e-12

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: 70.43  E-value: 1.54e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 144 ETPLFTAAEKGNIDVVKELLPYTTIEsLMQKNLSGFDALHIACSQGHRSIVQLLLEHEPQLsktvaqsnatplvsaatrg 223
Cdd:cd22192   18 ESPLLLAAKENDVQAIKKLLKCPSCD-LFQRGALGETALHVAALYDNLEAAVVLMEAAPEL------------------- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 224 hsevVNEllAKDSSLLEisrsnGKNALHLAARQGHVDIVRTLLDK--DPQLARRTD---KKGQTSL-----HM----AVK 289
Cdd:cd22192   78 ----VNE--PMTSDLYQ-----GETALHIAVVNQNLNLVRELIARgaDVVSPRATGtffRPGPKNLiyygeHPlsfaACV 146
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 240255309 290 GvSSQVVRLLLRADPAIVMlPDKFGNTVLHI----ATRKKRAEIVNELLQLpDTNVNALTRDHKTAYDiaeGLT 359
Cdd:cd22192  147 G-NEEIVRLLIEHGADIRA-QDSLGNTVLHIlvlqPNKTFACQMYDLILSY-DKEDDLQPLDLVPNNQ---GLT 214
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
95-321 6.01e-10

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 62.41  E-value: 6.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309   95 AAQRGDLASVKQILsdidsqitgtitgadfddevAQIMTSVVNEVNELGETPLFTAAEKGNIDVVKELLPYTTIESLMQK 174
Cdd:TIGR00870  24 AAERGDLASVYRDL--------------------EEPKKLNINCPDRLGRSALFVAAIENENLELTELLLNLSCRGAVGD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309  175 NLsgfdaLHIAcSQGHRSIVQLLLEHEPQLsktvaqsnatplvsaatrgHSEVVNELLAKDSSLLEISRsnGKNALHLAA 254
Cdd:TIGR00870  84 TL-----LHAI-SLEYVDAVEAILLHLLAA-------------------FRKSGPLELANDQYTSEFTP--GITALHLAA 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309  255 RQGHVDIVRTLLDKDPQLARR------TDKKGQTSLHM------AVKGVSS-QVVRLLLRaDPAIVMLPDKFGNTVLHIA 321
Cdd:TIGR00870 137 HRQNYEIVKLLLERGASVPARacgdffVKSQGVDSFYHgesplnAAACLGSpSIVALLSE-DPADILTADSLGNTLLHLL 215
Ank_5 pfam13857
Ankyrin repeats (many copies);
265-321 1.88e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.81  E-value: 1.88e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 240255309  265 LLDKDPQLARRTDKKGQTSLHMAVKGVSSQVVRLLLRADPAIvMLPDKFGNTVLHIA 321
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDL-NLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
248-300 2.41e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.65  E-value: 2.41e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 240255309  248 NALHLAARQGHVDIVRTLLDKDPQLArRTDKKGQTSLHMAVKGVSSQVVRLLL 300
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADIN-AVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
136-387 4.70e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 52.66  E-value: 4.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 136 VNEVNELGETPLFTAAEKGNIDVVKEL---------LPYTTIESLMQKNL--SGFDA----------LHIACSQGHRSIV 194
Cdd:PHA02874  61 INHINTKIPHPLLTAIKIGAHDIIKLLidngvdtsiLPIPCIEKDMIKTIldCGIDVnikdaelktfLHYAIKKGDLESI 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 195 QLLLEHEPQLSktVAQSNATPLVSAATRGHSEVVNELLAKDSSLLEISRSNGKNALHLAARQGHVDIVRTLLDKDPQLAR 274
Cdd:PHA02874 141 KMLFEYGADVN--IEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMN 218
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 275 RTdKKGQTSLHMAVKGVSSqVVRLLLraDPAIVMLPDKFGNTVLHIATRKK-RAEIVNELLQlpdTNVNALTRDHKTAYD 353
Cdd:PHA02874 219 KC-KNGFTPLHNAIIHNRS-AIELLI--NNASINDQDIDGSTPLHHAINPPcDIDIIDILLY---HKADISIKDNKGENP 291
                        250       260       270
                 ....*....|....*....|....*....|....
gi 240255309 354 IAEGLTHSEETAEIKEILSrcGALKANELNQPRD 387
Cdd:PHA02874 292 IDTAFKYINKDPVIKDIIA--NAVLIKEADKLKD 323
Ank_4 pfam13637
Ankyrin repeats (many copies);
145-198 7.01e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.50  E-value: 7.01e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 240255309  145 TPLFTAAEKGNIDVVKELLPYTTieSLMQKNLSGFDALHIACSQGHRSIVQLLL 198
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGA--DINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02741 PHA02741
hypothetical protein; Provisional
228-356 7.78e-07

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 49.27  E-value: 7.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 228 VNELLAKDSSLLEISRSNGKNALHLAARQGHVDIVRTLL-----DKDPQLARRTDKKGQTSLHMAV----KGVSSQVVRL 298
Cdd:PHA02741   3 SPHFMTCLEEMIAEKNSEGENFFHEAARCGCFDIIARFTpfirgDCHAAALNATDDAGQMCIHIAAekheAQLAAEIIDH 82
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 240255309 299 LLRADPAIVMLPDKFGNTVLHIATRKKRAEIVNELLQLPDTNVNALTRDHKTAYDIAE 356
Cdd:PHA02741  83 LIELGADINAQEMLEGDTALHLAAHRRDHDLAEWLCCQPGIDLHFCNADNKSPFELAI 140
Ank_5 pfam13857
Ankyrin repeats (many copies);
299-355 8.12e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.19  E-value: 8.12e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 240255309  299 LLRADPAIVMLPDKFGNTVLHIATRKKRAEIVNELLQLPdTNVNALTRDHKTAYDIA 355
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYG-VDLNLKDEEGLTALDLA 56
PHA02875 PHA02875
ankyrin repeat protein; Provisional
154-334 8.20e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 51.53  E-value: 8.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 154 GNIDVVKELLpyttiESLMQKNLS---GFDALHIACSQGHRSIVQLLLEHE--PQLSKTVAQSnatPLVSAATRGHSEVV 228
Cdd:PHA02875  13 GELDIARRLL-----DIGINPNFEiydGISPIKLAMKFRDSEAIKLLMKHGaiPDVKYPDIES---ELHDAVEEGDVKAV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 229 NELLAKDSSLLEISRSNGKNALHLAARQGHVDIVRTLLDK--DPQLArRTDKKgqTSLHMAVKGVSSQVVRLLLRaDPAI 306
Cdd:PHA02875  85 EELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARgaDPDIP-NTDKF--SPLHLAVMMGDIKGIELLID-HKAC 160
                        170       180
                 ....*....|....*....|....*...
gi 240255309 307 VMLPDKFGNTVLHIATRKKRAEIVNELL 334
Cdd:PHA02875 161 LDIEDCCGCTPLIIAMAKGDIAICKMLL 188
PHA02736 PHA02736
Viral ankyrin protein; Provisional
246-355 9.97e-07

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 48.72  E-value: 9.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 246 GKNALHLAARQGHV-DIV---RTLLDKDPQLARRTDKKGQTSLHMAV---KGVSSQVVRLLLRADPAIVMLPDKFGNTVL 318
Cdd:PHA02736  17 GENILHYLCRNGGVtDLLafkNAISDENRYLVLEYNRHGKQCVHIVSnpdKADPQEKLKLLMEWGADINGKERVFGNTPL 96
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 240255309 319 HIATRKKRAEIVNELLQLPDTNVNALTRDHKTAYDIA 355
Cdd:PHA02736  97 HIAVYTQNYELATWLCNQPGVNMEILNYAFKTPYYVA 133
PHA02875 PHA02875
ankyrin repeat protein; Provisional
89-268 1.22e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 51.15  E-value: 1.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309  89 DTELHLAAQRGDLASVKQILsdidsqITGTitgadFDDEVaqimtsvvneVNELGETPLFTAAEKGNIDVVKELLPYTTI 168
Cdd:PHA02875  69 ESELHDAVEEGDVKAVEELL------DLGK-----FADDV----------FYKDGMTPLHLATILKKLDIMKLLIARGAD 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 169 ESLmqKNLSGFDALHIACSQGHRSIVQLLLEHEPQLSKTVAqSNATPLVSAATRGHSEVVNELLAKDSSLLEISRSNGKN 248
Cdd:PHA02875 128 PDI--PNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDC-CGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVA 204
                        170       180
                 ....*....|....*....|
gi 240255309 249 ALHLAARQGHVDIVRTLLDK 268
Cdd:PHA02875 205 ALCYAIENNKIDIVRLFIKR 224
Ank_5 pfam13857
Ankyrin repeats (many copies);
231-287 1.91e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.03  E-value: 1.91e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 240255309  231 LLAKDSSLLEISRSNGKNALHLAARQGHVDIVRTLLDKdPQLARRTDKKGQTSLHMA 287
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAY-GVDLNLKDEEGLTALDLA 56
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
104-355 1.96e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 51.02  E-value: 1.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 104 VKQILSD-IDSQITGTITGADFDDEVAQI---------MTSVVNEVNELGETPLFTAAE---KGNIDVVKELLPYtties 170
Cdd:PLN03192 426 VEIIDSEgEKERVVGTLGCGDIFGEVGALccrpqsftfRTKTLSQLLRLKTSTLIEAMQtrqEDNVVILKNFLQH----- 500
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 171 lmQKNLSGFDalhiacsqghrsIVQLLLEHEPQLSKTVAQSNatpLVSAATRGHSEVVNELL-AKDSSllEISRSNGKNA 249
Cdd:PLN03192 501 --HKELHDLN------------VGDLLGDNGGEHDDPNMASN---LLTVASTGNAALLEELLkAKLDP--DIGDSKGRTP 561
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 250 LHLAARQGHVDIVRTLLDKDPQLARRtDKKGQTSLHMAVKGVSSQVVRLLLR----ADPAIvmlpdkfGNTVLHIATRKK 325
Cdd:PLN03192 562 LHIAASKGYEDCVLVLLKHACNVHIR-DANGNTALWNAISAKHHKIFRILYHfasiSDPHA-------AGDLLCTAAKRN 633
                        250       260       270
                 ....*....|....*....|....*....|
gi 240255309 326 RAEIVNELLQLpDTNVNALTRDHKTAYDIA 355
Cdd:PLN03192 634 DLTAMKELLKQ-GLNVDSEDHQGATALQVA 662
Ank_4 pfam13637
Ankyrin repeats (many copies);
214-266 3.57e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.19  E-value: 3.57e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 240255309  214 TPLVSAATRGHSEVVNELLAKDSSLLEISRsNGKNALHLAARQGHVDIVRTLL 266
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDG-NGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
284-355 3.95e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 45.49  E-value: 3.95e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 240255309  284 LHMAVKGVSSQVVRLLLRADPAIvMLPDKFGNTVLHIATRKKRAEIVNELLQLPDTNVNAltrDHKTAYDIA 355
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADA-NLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD---NGRTALHYA 68
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
86-268 6.22e-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: 49.24  E-value: 6.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309  86 RHNDTELHLAAQRGDLASVKQIL--SDIDSQITGTI------TGADFD-DEVAQIMTSVVNE-VNE-------LGETPLF 148
Cdd:cd22192   15 RISESPLLLAAKENDVQAIKKLLkcPSCDLFQRGALgetalhVAALYDnLEAAVVLMEAAPElVNEpmtsdlyQGETALH 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 149 TAAEKGNIDVVKELLPYT----------TIESLMQKNLS--GFDALHIACSQGHRSIVQLLLEH------EPQLSKTV-- 208
Cdd:cd22192   95 IAVVNQNLNLVRELIARGadvvspratgTFFRPGPKNLIyyGEHPLSFAACVGNEEIVRLLIEHgadiraQDSLGNTVlh 174
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 240255309 209 ---AQSNATPLvsaatrghSEVVNELLAKDSSLLEISRSNGKN-----ALHLAARQGHVDIVRTLLDK 268
Cdd:cd22192  175 ilvLQPNKTFA--------CQMYDLILSYDKEDDLQPLDLVPNnqgltPFKLAAKEGNIVMFQHLVQK 234
PHA02878 PHA02878
ankyrin repeat protein; Provisional
146-343 7.07e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 48.72  E-value: 7.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 146 PLFTAAEKGNIDVVKELLpyTTIESLMQKNLSGFDALHIACSQGH--------RSIVQLLLEHEPQLSKTVAQSN----- 212
Cdd:PHA02878  40 PLHQAVEARNLDVVKSLL--TRGHNVNQPDHRDLTPLHIICKEPNklgmkemiRSINKCSVFYTLVAIKDAFNNRnveif 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 213 ------------ATPLVSAATRGH-----SEVVNELLAKDSSLLEISRSNGKNALHLAARQGHVDIVRTLLDK--DPQLA 273
Cdd:PHA02878 118 kiiltnrykniqTIDLVYIDKKSKddiieAEITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYgaNVNIP 197
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 240255309 274 RRTDKkgqTSLHMAVKGVSSQVVRLLLRaDPAIVMLPDKFGNTVLHIAT-RKKRAEIVNELLQlPDTNVNA 343
Cdd:PHA02878 198 DKTNN---SPLHHAVKHYNKPIVHILLE-NGASTDARDKCGNTPLHISVgYCKDYDILKLLLE-HGVDVNA 263
Ank_4 pfam13637
Ankyrin repeats (many copies);
180-232 1.33e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.65  E-value: 1.33e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 240255309  180 DALHIACSQGHRSIVQLLLEHEPQLSKTVAQSNaTPLVSAATRGHSEVVNELL 232
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGE-TALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
143-266 3.04e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 47.17  E-value: 3.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 143 GETPLFTAAEKGNIDVVKELLPYTTieSLMQKNLSGFDALHIACSQGHRSIVQLLLeHEPQLSKTVAQSNAtpLVSAATR 222
Cdd:PLN03192 558 GRTPLHIAASKGYEDCVLVLLKHAC--NVHIRDANGNTALWNAISAKHHKIFRILY-HFASISDPHAAGDL--LCTAAKR 632
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 240255309 223 GHSEVVNELLaKDSSLLEISRSNGKNALHLAARQGHVDIVRTLL 266
Cdd:PLN03192 633 NDLTAMKELL-KQGLNVDSEDHQGATALQVAMAEDHVDMVRLLI 675
PHA02743 PHA02743
Viral ankyrin protein; Provisional
247-376 3.57e-05

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 44.42  E-value: 3.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 247 KNALHLAARQGHVDI---VRTLLDKDPQLARRTDKKGQTSLHMAVK-GVSSQVVR--LLLRADPAIVMLPDKFGNTVLHI 320
Cdd:PHA02743  21 QNTFLRICRTGNIYElmeVAPFISGDGHLLHRYDHHGRQCTHMVAWyDRANAVMKieLLVNMGADINARELGTGNTLLHI 100
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 240255309 321 ATRKKRAEIVNELLQLPDTNVNALTRDHKTAYDIAegltHSEETAEIKEILSRCGA 376
Cdd:PHA02743 101 AASTKNYELAEWLCRQLGVNLGAINYQHETAYHIA----YKMRDRRMMEILRANGA 152
PHA02874 PHA02874
ankyrin repeat protein; Provisional
86-341 4.03e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 46.50  E-value: 4.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309  86 RHNDTELHLAAQRGDLASVKQILSdidsqitgtiTGADfddevaqimtsvVNEVNELGETPLFTAAEKGNIDVVKELLPY 165
Cdd:PHA02874 122 AELKTFLHYAIKKGDLESIKMLFE----------YGAD------------VNIEDDNGCYPIHIAIKHNFFDIIKLLLEK 179
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 166 TTIESLmqKNLSGFDALHIACSQGHRSIVQLLLEHEPQLSKTvAQSNATPLVSAATrgHSEVVNELLAKDSSlLEISRSN 245
Cdd:PHA02874 180 GAYANV--KDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNK-CKNGFTPLHNAII--HNRSAIELLINNAS-INDQDID 253
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 246 GKNALHLAARQG-HVDIVRTLLDKDPQLARRtDKKGQTSLHMAVKGVSSQVVrlllradpaivmLPDKFGNTVLhiatrk 324
Cdd:PHA02874 254 GSTPLHHAINPPcDIDIIDILLYHKADISIK-DNKGENPIDTAFKYINKDPV------------IKDIIANAVL------ 314
                        250
                 ....*....|....*..
gi 240255309 325 kraeiVNELLQLPDTNV 341
Cdd:PHA02874 315 -----IKEADKLKDSDF 326
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
245-270 1.71e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.11  E-value: 1.71e-04
                           10        20
                   ....*....|....*....|....*.
gi 240255309   245 NGKNALHLAARQGHVDIVRTLLDKDP 270
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
245-301 1.93e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.50  E-value: 1.93e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 240255309 245 NGKNALHLAARQGHVDIVRTLLD--KDPQLarrTDKKGQTSLHMAVKGVSSQVVRLLLR 301
Cdd:PTZ00322 114 DGRTPLHIACANGHVQVVRVLLEfgADPTL---LDKDGKTPLELAEENGFREVVQLLSR 169
Ank_5 pfam13857
Ankyrin repeats (many copies);
197-253 4.54e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.48  E-value: 4.54e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 240255309  197 LLEHEPQLSKTVAQSNATPLVSAATRGHSEVVNELLAKDSSLLeISRSNGKNALHLA 253
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLN-LKDEEGLTALDLA 56
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
160-320 7.86e-04

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 42.56  E-value: 7.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 160 KELLPY------TTIESLMQKNLSGFDALHIAcsqghrsivqLLLEHEPQLSKtvaqsnATPLVSAA--TRGHSEVVNEL 231
Cdd:cd21882    2 EELLGLleclrwYLTDSAYQRGATGKTCLHKA----------ALNLNDGVNEA------IMLLLEAApdSGNPKELVNAP 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 232 LAkdSSLLEisrsnGKNALHLAARQGHVDIVRTLLDK--DPQLA------RRTDKK----GQTSLHMAVKGVSSQVVRLL 299
Cdd:cd21882   66 CT--DEFYQ-----GQTALHIAIENRNLNLVRLLVENgaDVSARatgrffRKSPGNlfyfGELPLSLAACTNQEEIVRLL 138
                        170       180
                 ....*....|....*....|...
gi 240255309 300 LR--ADPAIVMLPDKFGNTVLHI 320
Cdd:cd21882  139 LEngAQPAALEAQDSLGNTVLHA 161
PHA03100 PHA03100
ankyrin repeat protein; Provisional
136-202 8.19e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 41.96  E-value: 8.19e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 240255309 136 VNEVNELGETPLFTAAEKGNIDVVKELLPYTTieSLMQKNLSGFDALHIACSQGHRSIVQLLLEHEP 202
Cdd:PHA03100 185 INIKDVYGFTPLHYAVYNNNPEFVKYLLDLGA--NPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249
PHA02876 PHA02876
ankyrin repeat protein; Provisional
136-348 9.09e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 42.36  E-value: 9.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 136 VNEVNELGETPLFTAAEKGNIDVVKELLPYTTIESLMqkNLSGFDALHIACSQGHRSIVQLLLEHEPQLSKtvaqsNATP 215
Cdd:PHA02876 171 VNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNII--ALDDLSVLECAVDSKNIDTIKAIIDNRSNINK-----NDLS 243
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 216 LVSAATrgHSEVVNELLAKDSSLLEISRSNGKNA-LHLAARQGHVD-IVRTLLDKDPQLARRtDKKGQTSLH-MAVKGVS 292
Cdd:PHA02876 244 LLKAIR--NEDLETSLLLYDAGFSVNSIDDCKNTpLHHASQAPSLSrLVPKLLERGADVNAK-NIKGETPLYlMAKNGYD 320
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 240255309 293 SQVVRLLLRADpAIVMLPDKFGNTVLHIA-TRKKRAEIVNELLQLpDTNVNAltRDH 348
Cdd:PHA02876 321 TENIRTLIMLG-ADVNAADRLYITPLHQAsTLDRNKDIVITLLEL-GANVNA--RDY 373
PRK11207 PRK11207
tellurite resistance methyltransferase TehB;
221-307 9.22e-04

tellurite resistance methyltransferase TehB;


Pssm-ID: 183040  Cd Length: 197  Bit Score: 40.87  E-value: 9.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 221 TRGHSEVVNEL-LAKDSSLLEISRSNGKNALHLAARQGHVdivrTLLDKDP----QLARRTDKKGQTSLHMAVKG----- 290
Cdd:PRK11207  16 TRTHSEVLEAVkVVKPGKTLDLGCGNGRNSLYLAANGFDV----TAWDKNPmsiaNLERIKAAENLDNLHTAVVDlnnlt 91
                         90       100
                 ....*....|....*....|....*.
gi 240255309 291 -------VSSQVVRLLLRAD--PAIV 307
Cdd:PRK11207  92 fdgeydfILSTVVLMFLEAKtiPGLI 117
Ank_4 pfam13637
Ankyrin repeats (many copies);
88-163 9.23e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.64  E-value: 9.23e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 240255309   88 NDTELHLAAQRGDLASVKQILSdidsqitgtiTGADfddevaqimtsvVNEVNELGETPLFTAAEKGNIDVVKELL 163
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLE----------KGAD------------INAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
251-334 2.36e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.04  E-value: 2.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 251 HLAARQGHVDIvRTLLDKDPQLARRtDKKGQTSLHMAVKGVSSQVVRLLLR--ADPAivmLPDKFGNTVLHIATRKKRAE 328
Cdd:PTZ00322  88 QLAASGDAVGA-RILLTGGADPNCR-DYDGRTPLHIACANGHVQVVRVLLEfgADPT---LLDKDGKTPLELAEENGFRE 162

                 ....*.
gi 240255309 329 IVNELL 334
Cdd:PTZ00322 163 VVQLLS 168
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
296-389 3.17e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 40.65  E-value: 3.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 296 VRLLLR--ADPAIVmlpDKFGNTVLHIATRKKRAEIVNELLQLpDTNVNALTRDHKTAYDIAEglthSEETAEIKEILSR 373
Cdd:PTZ00322  98 ARILLTggADPNCR---DYDGRTPLHIACANGHVQVVRVLLEF-GADPTLLDKDGKTPLELAE----ENGFREVVQLLSR 169
                         90
                 ....*....|....*..
gi 240255309 374 CGALKAN-ELNQPRDEL 389
Cdd:PTZ00322 170 HSQCHFElGANAKPDSF 186
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
245-272 3.20e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 35.31  E-value: 3.20e-03
                          10        20
                  ....*....|....*....|....*...
gi 240255309  245 NGKNALHLAARQGHVDIVRTLLDKDPQL 272
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
245-277 3.79e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.34  E-value: 3.79e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 240255309  245 NGKNALHLAA-RQGHVDIVRTLLDKDPQLARRTD 277
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA03095 PHA03095
ankyrin-like protein; Provisional
226-354 3.81e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 40.01  E-value: 3.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 226 EVVNELLAKDSSLlEISRSNGKNALHLAARQGH---VDIVRTLLDKDPQLARRtDKKGQTSLHMAVK-GVSSQVVRLLLR 301
Cdd:PHA03095  28 EEVRRLLAAGADV-NFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAP-ERCGFTPLHLYLYnATTLDVIKLLIK 105
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 240255309 302 ADpAIVMLPDKFGNTVLHIATRKK--RAEIVNELLQLpDTNVNALTRDHKTAYDI 354
Cdd:PHA03095 106 AG-ADVNAKDKVGRTPLHVYLSGFniNPKVIRLLLRK-GADVNALDLYGMTPLAV 158
NAM-associated pfam14303
No apical meristem-associated C-terminal domain; This domain is found in a number of different ...
20-107 6.85e-03

No apical meristem-associated C-terminal domain; This domain is found in a number of different types of plant proteins including NAM-like proteins.


Pssm-ID: 464129  Cd Length: 142  Bit Score: 37.46  E-value: 6.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309   20 ATDPTSPTGSTVADLSPTPTPRKTLVLSNSGKALMVSNSSKSLGLSNSGKRfdPTGKKKY---VKQVTGRHNDTELHLAA 96
Cdd:pfam14303  27 NKKPSSTASSSPAPTSLASTDPDTDSSDSSSAGSNESNSDDSSPSSKSPTR--PIGRKKAkekRQEELDAAKEEKKQNDI 104
                          90
                  ....*....|.
gi 240255309   97 QRGDLASVKQI 107
Cdd:pfam14303 105 EEAQVAAELRL 115
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
178-200 9.05e-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: 9.05e-03
                           10        20
                   ....*....|....*....|...
gi 240255309   178 GFDALHIACSQGHRSIVQLLLEH 200
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDK 24
 
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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