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Conserved domains on  [gi|1169100650|ref|NP_001336782|]
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ankyrin repeat domain-containing protein 54 isoform 2 [Homo sapiens]

Protein Classification

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

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

Gene Ontology:  GO:0005515
PubMed:  33435370|17176038

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
49-151 5.69e-32

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 118.13  E-value: 5.69e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100650  49 LRDSANANDVETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQRDGLGNTPLHLAACTNHVPVIT 128
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                          90       100
                  ....*....|....*....|...
gi 1169100650 129 TLLRGGARVDALDRAGRTPLHLA 151
Cdd:COG0666   171 LLLEAGADVNARDNDGETPLHLA 193
PLN03192 super family cl33658
Voltage-dependent potassium channel; Provisional
 89-235 7.73e-05

Voltage-dependent potassium channel; Provisional


The actual alignment was detected with superfamily member PLN03192:

Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 43.32  E-value: 7.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100650  89 GNDQIVQLLLDHGADPNQRDGLGNTPLHLAACTNHVPVITTLLRGGARVDALDRAGRTPLHLAKSK-----LNILQE--- 160
Cdd:PLN03192  536 GNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAkhhkiFRILYHfas 615

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100650 161 -------GHAQCLEAVRLEVKqiihMLREYLeRLGQHEQRERLDDLcTRLQMTSTKEQVDEVTDLL---ASFTSLSL--Q 228
Cdd:PLN03192  616 isdphaaGDLLCTAAKRNDLT----AMKELL-KQGLNVDSEDHQGA-TALQVAMAEDHVDMVRLLImngADVDKANTddD 689


                  ....*..
gi 1169100650 229 MQSMEKR 235
Cdd:PLN03192  690 FSPTELR 696
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
49-151 5.69e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 118.13  E-value: 5.69e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100650  49 LRDSANANDVETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQRDGLGNTPLHLAACTNHVPVIT 128
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                          90       100
                  ....*....|....*....|...
gi 1169100650 129 TLLRGGARVDALDRAGRTPLHLA 151
Cdd:COG0666   171 LLLEAGADVNARDNDGETPLHLA 193
Ank_2 pfam12796
Ankyrin repeats (3 copies);
53-141 3.77e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 81.70  E-value: 3.77e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100650  53 ANANDVETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHgADPNQRDGlGNTPLHLAACTNHVPVITTLLR 132
Cdd:pfam12796   5 AKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLLE 82


                  ....*....
gi 1169100650 133 GGARVDALD 141
Cdd:pfam12796  83 KGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 52-151 5.45e-19

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 85.08  E-value: 5.45e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100650  52 SANANdVETVQQLLEDGADPCAADDKGRTALH-FA-SCNGNDQIVQLLLDHGADPNQRDGLGNTPLHLAA--CTNHVPVI 127
Cdd:PHA03095  162 SRNAN-VELLRLLIDAGADVYAVDDRFRSLLHhHLqSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMAtgSSCKRSLV 240

                          90       100
                  ....*....|....*....|....
gi 1169100650 128 TTLLRGGARVDALDRAGRTPLHLA 151
Cdd:PHA03095  241 LPLLIAGISINARNRYGQTPLHYA 264
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 56-157 2.00e-11

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 63.11  E-value: 2.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100650  56 NDVETVQQLLEDGADPCAAD------DKGRTAL-----H---FASCNGNDQIVQLLLDHGADPNQRDGLGNTPLH-LAAC 120
Cdd:cd22192   100 QNLNLVRELIARGADVVSPRatgtffRPGPKNLiyygeHplsFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHiLVLQ 179

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1169100650 121 TNHVPV------ITTLLRGG--ARVDAL-DRAGRTPLHLAKSKLNI 157
Cdd:cd22192   180 PNKTFAcqmydlILSYDKEDdlQPLDLVpNNQGLTPFKLAAKEGNI 225
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 56-157 1.20e-06

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 48.92  E-value: 1.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100650  56 NDVETVQQLLEDGAD---PCAADD-----------KGRTALHFASCNGNDQIVQLLLDHGADPNQRDGLGNTPLHLAACT 121
Cdd:TIGR00870 139 QNYEIVKLLLERGASvpaRACGDFfvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVME 218

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1169100650 122 NHVPVITT---------LLRGGARVDA-------LDRAGRTPLHLAKSKLNI 157
Cdd:TIGR00870 219 NEFKAEYEelscqmynfALSLLDKLRDskeleviLNHQGLTPLKLAAKEGRI 270
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 77-105 1.21e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 43.73  E-value: 1.21e-06
                           10        20
                   ....*....|....*....|....*....
gi 1169100650   77 KGRTALHFASCNGNDQIVQLLLDHGADPN 105
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 89-235 7.73e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 43.32  E-value: 7.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100650  89 GNDQIVQLLLDHGADPNQRDGLGNTPLHLAACTNHVPVITTLLRGGARVDALDRAGRTPLHLAKSK-----LNILQE--- 160
Cdd:PLN03192  536 GNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAkhhkiFRILYHfas 615

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100650 161 -------GHAQCLEAVRLEVKqiihMLREYLeRLGQHEQRERLDDLcTRLQMTSTKEQVDEVTDLL---ASFTSLSL--Q 228
Cdd:PLN03192  616 isdphaaGDLLCTAAKRNDLT----AMKELL-KQGLNVDSEDHQGA-TALQVAMAEDHVDMVRLLImngADVDKANTddD 689


                  ....*..
gi 1169100650 229 MQSMEKR 235
Cdd:PLN03192  690 FSPTELR 696
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
49-151 5.69e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 118.13  E-value: 5.69e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100650  49 LRDSANANDVETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQRDGLGNTPLHLAACTNHVPVIT 128
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                          90       100
                  ....*....|....*....|...
gi 1169100650 129 TLLRGGARVDALDRAGRTPLHLA 151
Cdd:COG0666   171 LLLEAGADVNARDNDGETPLHLA 193
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
53-156 1.74e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 116.98  E-value: 1.74e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100650  53 ANANDVETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQRDGLGNTPLHLAACTNHVPVITTLLR 132
Cdd:COG0666   128 AYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLE 207

                          90       100
                  ....*....|....*....|....
gi 1169100650 133 GGARVDALDRAGRTPLHLAKSKLN 156
Cdd:COG0666   208 AGADVNAKDNDGKTALDLAAENGN 231
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
49-151 8.26e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 96.56  E-value: 8.26e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100650  49 LRDSANANDVETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQRDGLGNTPLHLAACTNHVPVIT 128
Cdd:COG0666    58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137

                          90       100
                  ....*....|....*....|...
gi 1169100650 129 TLLRGGARVDALDRAGRTPLHLA 151
Cdd:COG0666   138 LLLEAGADVNAQDNDGNTPLHLA 160
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
53-164 5.24e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 94.25  E-value: 5.24e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100650  53 ANANDVETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQRDGLGNTPLHLAACTNHVPVITTLLR 132
Cdd:COG0666   161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1169100650 133 GGARVDALDRAGRTPLHLAKSKLNILQEGHAQ 164
Cdd:COG0666   241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLL 272
Ank_2 pfam12796
Ankyrin repeats (3 copies);
53-141 3.77e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 81.70  E-value: 3.77e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100650  53 ANANDVETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHgADPNQRDGlGNTPLHLAACTNHVPVITTLLR 132
Cdd:pfam12796   5 AKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLLE 82


                  ....*....
gi 1169100650 133 GGARVDALD 141
Cdd:pfam12796  83 KGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 52-151 5.45e-19

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 85.08  E-value: 5.45e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100650  52 SANANdVETVQQLLEDGADPCAADDKGRTALH-FA-SCNGNDQIVQLLLDHGADPNQRDGLGNTPLHLAA--CTNHVPVI 127
Cdd:PHA03095  162 SRNAN-VELLRLLIDAGADVYAVDDRFRSLLHhHLqSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMAtgSSCKRSLV 240

                          90       100
                  ....*....|....*....|....
gi 1169100650 128 TTLLRGGARVDALDRAGRTPLHLA 151
Cdd:PHA03095  241 LPLLIAGISINARNRYGQTPLHYA 264
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 57-155 2.00e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 80.31  E-value: 2.00e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100650  57 DVETVQQLLEDGADPCAAD-DKGRTALHFASCNGNDQIVQLLLDHGADPNQRDGLGNTPLHLAACTNHVPVITTLLRGGA 135
Cdd:PHA02878  146 EAEITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225

                          90       100
                  ....*....|....*....|
gi 1169100650 136 RVDALDRAGRTPLHLAKSKL 155
Cdd:PHA02878  226 STDARDKCGNTPLHISVGYC 245
PHA03095 PHA03095
ankyrin-like protein; Provisional
 52-179 4.27e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 79.30  E-value: 4.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100650  52 SANANDVETVQQLLEDGADPCAADDKGRTALHFASCNGND-QIVQLLLDHGADPNQRDGLGNTPLHlAACTN---HVPVI 127
Cdd:PHA03095   57 YSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGADVNAKDKVGRTPLH-VYLSGfniNPKVI 135

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1169100650 128 TTLLRGGARVDALDRAGRTPLHlaksklnILQEGHAQCLEAVRLEVKQIIHM 179
Cdd:PHA03095  136 RLLLRKGADVNALDLYGMTPLA-------VLLKSRNANVELLRLLIDAGADV 180
Ank_2 pfam12796
Ankyrin repeats (3 copies);
82-167 1.50e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 69.37  E-value: 1.50e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100650  82 LHFASCNGNDQIVQLLLDHGADPNQRDGLGNTPLHLAACTNHVPVITTLLRgGARVDALDRaGRTPLHLAksklniLQEG 161
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYA------ARSG 72


                  ....*.
gi 1169100650 162 HAQCLE 167
Cdd:pfam12796  73 HLEIVK 78
PHA03095 PHA03095
ankyrin-like protein; Provisional
 46-157 2.71e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 74.29  E-value: 2.71e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100650  46 LKRLRDSANAnDVETVQQLLEDGADPCAADDKGRTALH-FASCNGND--QIVQLLLDHGADPNQRDGLGNTPLHLAACTN 122
Cdd:PHA03095   16 YDYLLNASNV-TVEEVRRLLAAGADVNFRGEYGKTPLHlYLHYSSEKvkDIVRLLLEAGADVNAPERCGFTPLHLYLYNA 94

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1169100650 123 HV-PVITTLLRGGARVDALDRAGRTPLHLAKSKLNI 157
Cdd:PHA03095   95 TTlDVIKLLIKAGADVNAKDKVGRTPLHVYLSGFNI 130
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 52-151 1.15e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 69.71  E-value: 1.15e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100650  52 SANANDVETVQQLLEDGADPCAADDKGRTALHFASC-NGNDQIVQLLLDHGADPNQRDGLGNTPLHLAACTNHVPVITTL 130
Cdd:PHA02876  315 AKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTL 394

                          90       100
                  ....*....|....*....|.
gi 1169100650 131 LRGGARVDALDRAGRTPLHLA 151
Cdd:PHA02876  395 LDYGADIEALSQKIGTALHFA 415
PHA03095 PHA03095
ankyrin-like protein; Provisional
 61-151 1.63e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 68.90  E-value: 1.63e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100650  61 VQQLLEDGADPCAADDKGRTALH----FASCNgnDQIVQLLLDHGADPNQRDGLGNTPLHLAACTNHVPVITTLLRGGAR 136
Cdd:PHA03095  205 VRELIRAGCDPAATDMLGNTPLHsmatGSSCK--RSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGAD 282

                          90
                  ....*....|....*
gi 1169100650 137 VDALDRAGRTPLHLA 151
Cdd:PHA03095  283 INAVSSDGNTPLSLM 297
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 59-151 1.67e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 68.84  E-value: 1.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100650  59 ETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQRDGLGNTPLHLAACTNHVPVITTLLRGGARVD 138
Cdd:PHA02874  105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184

                          90
                  ....*....|...
gi 1169100650 139 ALDRAGRTPLHLA 151
Cdd:PHA02874  185 VKDNNGESPLHNA 197
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
39-151 6.39e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 66.52  E-value: 6.39e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100650  39 ARGNPQALKRLRDSANANDVETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQRDGLGNTPLHLA 118
Cdd:COG0666    15 LLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAA 94

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1169100650 119 ACTNHVPVITTLLRGGARVDALDRAGRTPLHLA 151
Cdd:COG0666    95 ARNGDLEIVKLLLEAGADVNARDKDGETPLHLA 127
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 44-151 6.95e-13

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 67.23  E-value: 6.95e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100650  44 QALKRLRDSANANDVETVQQLLEDGADPCAADDKGRTALHFAScNGNDQIVQLLLDHGADPNQRDGLGNTPLHLAACTNH 123
Cdd:PTZ00322   49 THLEALEATENKDATPDHNLTTEEVIDPVVAHMLTVELCQLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGH 127

                          90       100
                  ....*....|....*....|....*...
gi 1169100650 124 VPVITTLLRGGARVDALDRAGRTPLHLA 151
Cdd:PTZ00322  128 VQVVRVLLEFGADPTLLDKDGKTPLELA 155
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 61-142 1.16e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 66.61  E-value: 1.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100650  61 VQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQRDGLGNTPLHLAACTNHVPVITTLLRGGARVDAL 140
Cdd:PHA03100  175 VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTI 254


                  ..
gi 1169100650 141 DR 142
Cdd:PHA03100  255 IE 256
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 61-158 2.00e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 65.86  E-value: 2.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100650  61 VQQLLEDGADPCAADDKGRTALHFASCNGND-QIVQLLLDHGADPNQRDGLGNTPLHLAACTN-HVPVITTLLRGGARVD 138
Cdd:PHA02876  290 VPKLLERGADVNAKNIKGETPLYLMAKNGYDtENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVN 369

                          90       100
                  ....*....|....*....|
gi 1169100650 139 ALDRAGRTPLHLAKSKLNIL 158
Cdd:PHA02876  370 ARDYCDKTPIHYAAVRNNVV 389
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
53-148 3.12e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 64.59  E-value: 3.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100650  53 ANANDVETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQRDGLGNTPLHLAACTNHVPVITTLLR 132
Cdd:COG0666   194 AENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLL 273

                          90
                  ....*....|....*.
gi 1169100650 133 GGARVDALDRAGRTPL 148
Cdd:COG0666   274 ALLLLAAALLDLLTLL 289
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 56-151 3.71e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 65.07  E-value: 3.71e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100650  56 NDVETVQQLLEDGADPCAADDKGRTALH-FASCNGND-QIVQLLLDHGADPNQ----------------RDGLGNTPLHL 117
Cdd:PHA03100  119 NSYSIVEYLLDNGANVNIKNSDGENLLHlYLESNKIDlKILKLLIDKGVDINAknrvnyllsygvpiniKDVYGFTPLHY 198

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1169100650 118 AACTNHVPVITTLLRGGARVDALDRAGRTPLHLA 151
Cdd:PHA03100  199 AVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIA 232
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 53-132 5.58e-12

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 64.53  E-value: 5.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100650  53 ANANDVETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQRDGLGNTPLHLAACTNHVPVITTLLR 132
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 50-159 6.71e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 64.30  E-value: 6.71e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100650  50 RDSANANDVETvqqLLEDGADPCAADDKGRTALHFASCNG-----NDQIVQLLLDHGADPNQRDGLGNTPLHLAACT--N 122
Cdd:PHA03100   43 KEARNIDVVKI---LLDNGADINSSTKNNSTPLHYLSNIKynltdVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksN 119

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1169100650 123 HVPVITTLLRGGARVDALDRAGRTPLHLA----KSKLNILQ 159
Cdd:PHA03100  120 SYSIVEYLLDNGANVNIKNSDGENLLHLYlesnKIDLKILK 160
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 56-157 2.00e-11

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 63.11  E-value: 2.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100650  56 NDVETVQQLLEDGADPCAAD------DKGRTAL-----H---FASCNGNDQIVQLLLDHGADPNQRDGLGNTPLH-LAAC 120
Cdd:cd22192   100 QNLNLVRELIARGADVVSPRatgtffRPGPKNLiyygeHplsFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHiLVLQ 179

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1169100650 121 TNHVPV------ITTLLRGG--ARVDAL-DRAGRTPLHLAKSKLNI 157
Cdd:cd22192   180 PNKTFAcqmydlILSYDKEDdlQPLDLVpNNQGLTPFKLAAKEGNI 225
PHA02946 PHA02946
ankyin-like protein; Provisional
 57-148 6.12e-11

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 61.61  E-value: 6.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100650  57 DVETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQRDGLGNTPLHLAACTNH--VPVITTLLRGG 134
Cdd:PHA02946   51 DERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYG 130

                          90
                  ....*....|....*
gi 1169100650 135 ARV-DALDRAGRTPL 148
Cdd:PHA02946  131 AKInNSVDEEGCGPL 145
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 56-151 6.92e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 61.13  E-value: 6.92e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100650  56 NDVETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQRDGLGNTPLHLAACTNHVPVITTLLRGGA 135
Cdd:PHA02874  135 GDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGN 214

                          90
                  ....*....|....*.
gi 1169100650 136 RVDALDRAGRTPLHLA 151
Cdd:PHA02874  215 HIMNKCKNGFTPLHNA 230
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 61-171 7.18e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 61.42  E-value: 7.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100650  61 VQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQRDGLGNTPL----------------HLAA----- 119
Cdd:PLN03192  541 LEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnaisakhhkifrilyHFASisdph 620

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1169100650 120 ------CT----NHVPVITTLLRGGARVDALDRAGRTPLHLAksklniLQEGHAqclEAVRL 171
Cdd:PLN03192  621 aagdllCTaakrNDLTAMKELLKQGLNVDSEDHQGATALQVA------MAEDHV---DMVRL 673
Ank_4 pfam13637
Ankyrin repeats (many copies);
78-131 1.80e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.97  E-value: 1.80e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1169100650  78 GRTALHFASCNGNDQIVQLLLDHGADPNQRDGLGNTPLHLAACTNHVPVITTLL 131
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 52-158 1.96e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 60.08  E-value: 1.96e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100650  52 SANANDVETVQQLLEDGADPCAADDKGRTALHFASCNGNDQI-VQLLLDHGADPNQRDGLGNTPLHLAACTNHVP-VITT 129
Cdd:PHA02876  382 AAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVNSKNKDLSTPLHYACKKNCKLdVIEM 461

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1169100650 130 LLRGGARVDALDRAGRTPLHLA---KSKLNIL 158
Cdd:PHA02876  462 LLDNGADVNAINIQNQYPLLIAleyHGIVNIL 493
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 43-157 4.13e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 58.85  E-value: 4.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100650  43 PQALKRLRDSANANDVETVQQLLEDGAdpcAADD----KGRTALHFASCNGNDQIVQLLLDHGADPNQRDGLGNTPLHLA 118
Cdd:PHA02875   66 PDIESELHDAVEEGDVKAVEELLDLGK---FADDvfykDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLA 142

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1169100650 119 ACTNHVPVITTLLRGGARVDALDRAGRTPLHLAKSKLNI 157
Cdd:PHA02875  143 VMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDI 181
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 77-149 4.27e-10

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: 59.05  E-value: 4.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100650  77 KGRTALHFASCNGNDQIVQLLLDHGADPNQR------------DG--LGNTPLHLAACTNHVPVITTLLRG---GARVDA 139
Cdd:cd22196    93 KGQTALHIAIERRNMHLVELLVQNGADVHARasgeffkkkkggPGfyFGELPLSLAACTNQLDIVKFLLENphsPADISA 172

                          90
                  ....*....|
gi 1169100650 140 LDRAGRTPLH 149
Cdd:cd22196   173 RDSMGNTVLH 182
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 44-137 1.18e-09

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 57.72  E-value: 1.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100650  44 QALKRLRDS-----ANANDVETVQQLLE-DGADPCAADDKGRTALHFASCNGNDQIVQLLLDhgADP---NQRDG----L 110
Cdd:cd22192    11 LQQKRISESplllaAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPelvNEPMTsdlyQ 88

                          90       100
                  ....*....|....*....|....*..
gi 1169100650 111 GNTPLHLAACTNHVPVITTLLRGGARV 137
Cdd:cd22192    89 GETALHIAVVNQNLNLVRELIARGADV 115
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 45-156 1.64e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 54.12  E-value: 1.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100650  45 ALKRLRDSANANDVETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQRD-GLGNTPLHLAACTNH 123
Cdd:PHA02878  101 TLVAIKDAFNNRNVEIFKIILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDrHKGNTALHYATENKD 180

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1169100650 124 VPVITTLLRGGARVDALDRAGRTPLHLAKSKLN 156
Cdd:PHA02878  181 QRLTELLLSYGANVNIPDKTNNSPLHHAVKHYN 213
Ank_5 pfam13857
Ankyrin repeats (many copies);
64-118 2.74e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.88  E-value: 2.74e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1169100650  64 LLEDG-ADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQRDGLGNTPLHLA 118
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 61-157 3.08e-08

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: 53.35  E-value: 3.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100650  61 VQQLLEDGAD-------------PCAADDKGRTALHFASCNGNDQIVQLLLDHGADP---NQRDGLGNTPLH-LAACTNH 123
Cdd:cd21882    89 VRLLVENGADvsaratgrffrksPGNLFYFGELPLSLAACTNQEEIVRLLLENGAQPaalEAQDSLGNTVLHaLVLQADN 168

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1169100650 124 VPVITT--------LLRGGARVDAL-------DRAGRTPLHLAKSKLNI 157
Cdd:cd21882   169 TPENSAfvcqmynlLLSYGAHLDPTqqleeipNHQGLTPLKLAAVEGKI 217
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 57-153 3.26e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 53.53  E-value: 3.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100650  57 DVETVQQLLEDGADPCAADDKGRTALHFASCNGN-DQIVQLLLDHGADPNQRDGLGNTPLHLAACTNH-VPVITTLLRGG 134
Cdd:PHA02876  252 DLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLG 331

                          90
                  ....*....|....*....
gi 1169100650 135 ARVDALDRAGRTPLHLAKS 153
Cdd:PHA02876  332 ADVNAADRLYITPLHQAST 350
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 77-149 3.38e-08

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: 53.35  E-value: 3.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100650  77 KGRTALHFASCNGNDQIVQLLLDHGAD-----------PNQRDGL--GNTPLHLAACTNHVPVITTLLRGGARVDAL--- 140
Cdd:cd21882    72 QGQTALHIAIENRNLNLVRLLVENGADvsaratgrffrKSPGNLFyfGELPLSLAACTNQEEIVRLLLENGAQPAALeaq 151


                  ....*....
gi 1169100650 141 DRAGRTPLH 149
Cdd:cd21882   152 DSLGNTVLH 160
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 57-144 3.86e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 53.07  E-value: 3.86e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100650  57 DVETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQRDGLGNTPLHLAACTNHVPVITTLLRGGAR 136
Cdd:PHA02875  114 KLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGAN 193


                  ....*...
gi 1169100650 137 VDALDRAG 144
Cdd:PHA02875  194 IDYFGKNG 201
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 57-148 4.19e-08

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 53.38  E-value: 4.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100650  57 DVETVQQLLEDGADPCAADDKGRTALH--FASCNGNDQIVQLLLDHGADPNQRDGLGNTPLH-----------LAACTNH 123
Cdd:PHA02716  296 DISVVYSFLQPGVKLHYKDSAGRTCLHqyILRHNISTDIIKLLHEYGNDLNEPDNIGNTVLHtylsmlsvvniLDPETDN 375

                          90       100
                  ....*....|....*....|....*...
gi 1169100650 124 ---VPVITTLLRGGARVDALDRAGRTPL 148
Cdd:PHA02716  376 dirLDVIQCLISLGADITAVNCLGYTPL 403
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 56-151 5.28e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 52.66  E-value: 5.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100650  56 NDVETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQRDGLGNTPLHLAACTNHVPVitTLLRGGA 135
Cdd:PHA02874  168 NFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAI--ELLINNA 245

                          90
                  ....*....|....*.
gi 1169100650 136 RVDALDRAGRTPLHLA 151
Cdd:PHA02874  246 SINDQDIDGSTPLHHA 261
PHA03095 PHA03095
ankyrin-like protein; Provisional
 61-143 7.73e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 52.33  E-value: 7.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100650  61 VQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQRDGLGNTPLHLAACTNHVPVITTLLRGGARVDAL 140
Cdd:PHA03095  240 VLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETV 319


                  ...
gi 1169100650 141 DRA 143
Cdd:PHA03095  320 AAT 322
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 77-149 1.50e-07

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: 51.33  E-value: 1.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100650  77 KGRTALHFASCNGNDQIVQLLLDHGADPN------------QRDG--LGNTPLHLAACTNHVPVITTLLRGG---ARVDA 139
Cdd:cd22193    75 EGQTALHIAIERRQGDIVALLVENGADVHahakgrffqpkyQGEGfyFGELPLSLAACTNQPDIVQYLLENEhqpADIEA 154

                          90
                  ....*....|
gi 1169100650 140 LDRAGRTPLH 149
Cdd:cd22193   155 QDSRGNTVLH 164
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 54-149 1.73e-07

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: 51.30  E-value: 1.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100650  54 NANDVETVQQLL----EDG-------ADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPN------------QRDG- 109
Cdd:cd22194   106 NENTKEIVRILLafaeENGildrfinAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNahakgvffnpkyKHEGf 185

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1169100650 110 -LGNTPLHLAACTNHVPVITTLL-RGGARVDALDRAGRTPLH 149
Cdd:cd22194   186 yFGETPLALAACTNQPEIVQLLMeKESTDITSQDSRGNTVLH 227
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 44-149 2.18e-07

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 51.01  E-value: 2.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100650  44 QALKRLRDSANAndveTVQQLLEDGADP----------CAAD-DKGRTALHFASCNGNDQIVQLLLDHGADPNQRDG--- 109
Cdd:cd22197    53 KAVLNLQDGVNA----CIMPLLEIDKDSgnpkplvnaqCTDEyYRGHSALHIAIEKRSLQCVKLLVENGADVHARACgrf 128

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1169100650 110 ----------LGNTPLHLAACTNHVPVITTLLRGG---ARVDALDRAGRTPLH 149
Cdd:cd22197   129 fqkkqgtcfyFGELPLSLAACTKQWDVVNYLLENPhqpASLQAQDSLGNTVLH 181
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 77-108 2.57e-07

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: 45.74  E-value: 2.57e-07
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1169100650  77 KGRTALHFASC-NGNDQIVQLLLDHGADPNQRD 108
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
Ank_4 pfam13637
Ankyrin repeats (many copies);
53-98 2.69e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.11  E-value: 2.69e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1169100650  53 ANANDVETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLL 98
Cdd:pfam13637   9 AASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 61-151 3.19e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 50.26  E-value: 3.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100650  61 VQQLLEDGADPCAADDKGRTALHFASCNGND-QIVQLLLDHGADPNQRDG-LGNTPLHLAActnHVP-VITTLLRGGARV 137
Cdd:PHA02878  217 VHILLENGASTDARDKCGNTPLHISVGYCKDyDILKLLLEHGVDVNAKSYiLGLTALHSSI---KSErKLKLLLEYGADI 293

                          90
                  ....*....|....
gi 1169100650 138 DALDRAGRTPLHLA 151
Cdd:PHA02878  294 NSLNSYKLTPLSSA 307
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 95-165 4.91e-07

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 47.95  E-value: 4.91e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1169100650  95 QLLLDHGADPNQRDGL-GNTPLHLAACTNHVPVITTLLRG-GARVDALDRAGRTPLHLAKSK-----LNILQEGHAQC 165
Cdd:PHA02736   75 KLLMEWGADINGKERVfGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERhdakmMNILRAKGAQC 152
PHA02946 PHA02946
ankyin-like protein; Provisional
 90-149 9.80e-07

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 48.90  E-value: 9.80e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100650  90 NDQIVQLLLDHGADPNQRDGLGNTPLHLAACTNHVPVITTLLRGGARVDALDRAGRTPLH 149
Cdd:PHA02946   51 DERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLY 110
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 56-157 1.20e-06

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 48.92  E-value: 1.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100650  56 NDVETVQQLLEDGAD---PCAADD-----------KGRTALHFASCNGNDQIVQLLLDHGADPNQRDGLGNTPLHLAACT 121
Cdd:TIGR00870 139 QNYEIVKLLLERGASvpaRACGDFfvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVME 218

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1169100650 122 NHVPVITT---------LLRGGARVDA-------LDRAGRTPLHLAKSKLNI 157
Cdd:TIGR00870 219 NEFKAEYEelscqmynfALSLLDKLRDskeleviLNHQGLTPLKLAAKEGRI 270
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 77-105 1.21e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 43.73  E-value: 1.21e-06
                           10        20
                   ....*....|....*....|....*....
gi 1169100650   77 KGRTALHFASCNGNDQIVQLLLDHGADPN 105
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 46-141 1.49e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.52  E-value: 1.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100650  46 LKRLRDSANANDVETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPN--QRDGLgnTPLHLAACTNH 123
Cdd:PHA02876  146 MKLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNiiALDDL--SVLECAVDSKN 223

                          90
                  ....*....|....*...
gi 1169100650 124 VPVITTLLRGGARVDALD 141
Cdd:PHA02876  224 IDTIKAIIDNRSNINKND 241
Ank_5 pfam13857
Ankyrin repeats (many copies);
97-151 1.90e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.87  E-value: 1.90e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1169100650  97 LLDHG-ADPNQRDGLGNTPLHLAACTNHVPVITTLLRGGARVDALDRAGRTPLHLA 151
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 77-105 1.48e-05

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 40.70  E-value: 1.48e-05
                          10        20
                  ....*....|....*....|....*....
gi 1169100650  77 KGRTALHFASCNGNDQIVQLLLDHGADPN 105
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 51-149 4.30e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 43.27  E-value: 4.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100650  51 DSANANdVETVQQLLEDGAD-PCAADDKGRTALH-FASCNGN--DQIVQLLLDHGADPNQRDGLGNTPLH--LAACTNHV 124
Cdd:PHA02859   60 EKDKVN-VEILKFLIENGADvNFKTRDNNLSALHhYLSFNKNvePEILKILIDSGSSITEEDEDGKNLLHmyMCNFNVRI 138

                          90       100
                  ....*....|....*....|....*
gi 1169100650 125 PVITTLLRGGARVDALDRAGRTPLH 149
Cdd:PHA02859  139 NVIKLLIDSGVSFLNKDFDNNNILY 163
Ank_4 pfam13637
Ankyrin repeats (many copies);
111-167 4.37e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.95  E-value: 4.37e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1169100650 111 GNTPLHLAACTNHVPVITTLLRGGARVDALDRAGRTPLHLAksklniLQEGHAQCLE 167
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFA------ASNGNVEVLK 51
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 49-151 6.08e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 43.41  E-value: 6.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100650  49 LRDSANANDVETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGAD-----------------------PN 105
Cdd:PHA02874   39 LIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDtsilpipciekdmiktildcgidVN 118

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1169100650 106 QRDGLGNTPLHLAACTNHVPVITTLLRGGARVDALDRAGRTPLHLA 151
Cdd:PHA02874  119 IKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIA 164
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 89-235 7.73e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 43.32  E-value: 7.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100650  89 GNDQIVQLLLDHGADPNQRDGLGNTPLHLAACTNHVPVITTLLRGGARVDALDRAGRTPLHLAKSK-----LNILQE--- 160
Cdd:PLN03192  536 GNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAkhhkiFRILYHfas 615

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100650 161 -------GHAQCLEAVRLEVKqiihMLREYLeRLGQHEQRERLDDLcTRLQMTSTKEQVDEVTDLL---ASFTSLSL--Q 228
Cdd:PLN03192  616 isdphaaGDLLCTAAKRNDLT----AMKELL-KQGLNVDSEDHQGA-TALQVAMAEDHVDMVRLLImngADVDKANTddD 689


                  ....*..
gi 1169100650 229 MQSMEKR 235
Cdd:PLN03192  690 FSPTELR 696
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 111-142 1.59e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.04  E-value: 1.59e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1169100650 111 GNTPLHLAAC-TNHVPVITTLLRGGARVDALDR 142
Cdd:pfam00023   2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 49-156 2.10e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 41.87  E-value: 2.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100650  49 LRDSANANDVETVQQLLEDGADPCAADDKGRTALHFASCNgNDQIVQLLLDHgADPNQRDGLGNTPLHLA---ACTnhVP 125
Cdd:PHA02874  194 LHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIH-NRSAIELLINN-ASINDQDIDGSTPLHHAinpPCD--ID 269

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1169100650 126 VITTLLRGGARVDALDRAGRTPLHLAKSKLN 156
Cdd:PHA02874  270 IIDILLYHKADISIKDNKGENPIDTAFKYIN 300
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 51-151 2.51e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 41.52  E-value: 2.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100650  51 DSANANDVETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQRDGLGNTPLHLAACTNHVPVITTL 130
Cdd:PHA02875    8 DAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEEL 87

                          90       100
                  ....*....|....*....|..
gi 1169100650 131 LRGGARV-DALDRAGRTPLHLA 151
Cdd:PHA02875   88 LDLGKFAdDVFYKDGMTPLHLA 109
TRPV4 cd22195
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed ...
 77-149 2.82e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed broadly in neuronal and non-neuronal cells. It is activated by various stimuli, including hypo-osmolarity, warm temperature, and chemical ligands. TRPV4 acts in physiological functions such as osmoregulation and thermoregulation. It also has a role in mechanosensation in the vascular endothelium and urinary tract, and in cell barrier formation in vascular and epidermal tissues. Knockout mice studies suggested the functional importance of TRPV4 in the central nervous system, nociception, and bone formation. TRPV4 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411979 [Multi-domain]  Cd Length: 733  Bit Score: 41.76  E-value: 2.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100650  77 KGRTALHFASCNGNDQIVQLLLDHGAD-----------PNQRDG---LGNTPLHLAACTNHVPVITTLLRGGARVDAL-- 140
Cdd:cd22195   136 RGQTALHIAIERRCKHYVELLVEKGADvhaqargrffqPKDEGGyfyFGELPLSLAACTNQPDIVHYLTENAHKKADLrr 215

                          90
                  ....*....|
gi 1169100650 141 -DRAGRTPLH 149
Cdd:cd22195   216 qDSRGNTVLH 225
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 52-103 3.45e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 41.19  E-value: 3.45e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1169100650  52 SANANDVETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGAD 103
Cdd:PHA03100  199 AVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 58-100 6.92e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 40.27  E-value: 6.92e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1169100650  58 VETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDH 100
Cdd:PTZ00322  128 VQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 111-139 1.33e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.26  E-value: 1.33e-03
                           10        20
                   ....*....|....*....|....*....
gi 1169100650  111 GNTPLHLAACTNHVPVITTLLRGGARVDA 139
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02791 PHA02791
ankyrin-like protein; Provisional
 49-98 2.53e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 38.10  E-value: 2.53e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1169100650  49 LRDSANANDVETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLL 98
Cdd:PHA02791   65 LHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGNMQTVKLFV 114
PHA02798 PHA02798
ankyrin-like protein; Provisional
 58-171 2.73e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 38.28  E-value: 2.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100650  58 VETVQQLLEDGADPCAADDKGRTAL-----HFASCNGNDQIVQLLLDHGADPNQRDGLGNTPLHLA---ACTNHVPVITT 129
Cdd:PHA02798   51 TDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLlsnGYINNLEILLF 130

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1169100650 130 LLRGGARVDALDRAGRTPLHLaksklnILQEGHAQCLEAVRL 171
Cdd:PHA02798  131 MIENGADTTLLDKDGFTMLQV------YLQSNHHIDIEIIKL 166
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 93-157 3.11e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 38.51  E-value: 3.11e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169100650  93 IVQLLLDHGADPNQRDGLGNTPLHLAACTNHVPVITTLLRGGARVDALDRAGRTPLHLAKSKLNI 157
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNI 224
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 37-103 3.16e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 38.31  E-value: 3.16e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1169100650  37 FEARGNPQAL-KRLRDSANANDVETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGAD 103
Cdd:PLN03192  613 FASISDPHAAgDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGAD 680
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 57-118 4.13e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 37.94  E-value: 4.13e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1169100650  57 DVETVQQLLEDGADPCAADD-KGRTALHFAScnGNDQIVQLLLDHGADPNQRDGLGNTPLHLA 118
Cdd:PHA02878  247 DYDILKLLLEHGVDVNAKSYiLGLTALHSSI--KSERKLKLLLEYGADINSLNSYKLTPLSSA 307
PHA02791 PHA02791
ankyrin-like protein; Provisional
 70-157 4.58e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 37.33  E-value: 4.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100650  70 DPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQRDglGNTPLHLAACTNHVPVITTLLRGGARVDALDRAGRTPLH 149
Cdd:PHA02791   22 DAFKADVHGHSALYYAIADNNVRLVCTLLNAGALKNLLE--NEFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALY 99


                  ....*...
gi 1169100650 150 LAKSKLNI 157
Cdd:PHA02791  100 YAVDSGNM 107
 
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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