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Conserved domains on  [gi|21450059|ref|NP_659098|]
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ankyrin repeat domain-containing protein 54 isoform 1 [Mus musculus]

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];
113-215 1.96e-33

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 123.91  E-value: 1.96e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450059 113 LRDSANANDVETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQQDGLGNTPLHLAACTNHVPVIT 192
Cdd:COG0666  91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                        90       100
                ....*....|....*....|...
gi 21450059 193 TLLRGGARVDALDRAGRTPLHLA 215
Cdd:COG0666 171 LLLEAGADVNARDNDGETPLHLA 193
PLN03192 super family cl33658
Voltage-dependent potassium channel; Provisional
 153-299 1.56e-04

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: 1.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450059  153 GNDQIVQLLLDHGADPNQQDGLGNTPLHLAACTNHVPVITTLLRGGARVDALDRAGRTPLHLAKSK-----LNILQE--- 224
Cdd:PLN03192 536 GNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAkhhkiFRILYHfas 615

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450059  225 -------GHSQCLEAVRLEVKqiihMLREYLeRLGRHEQRERLDDLcTRLQMTSTKEQVDEVTDLL---ASFTSLSL--Q 292
Cdd:PLN03192 616 isdphaaGDLLCTAAKRNDLT----AMKELL-KQGLNVDSEDHQGA-TALQVAMAEDHVDMVRLLImngADVDKANTddD 689


                 ....*..
gi 21450059  293 MQSMEKR 299
Cdd:PLN03192 690 FSPTELR 696
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
113-215 1.96e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 123.91  E-value: 1.96e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450059 113 LRDSANANDVETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQQDGLGNTPLHLAACTNHVPVIT 192
Cdd:COG0666  91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                        90       100
                ....*....|....*....|...
gi 21450059 193 TLLRGGARVDALDRAGRTPLHLA 215
Cdd:COG0666 171 LLLEAGADVNARDNDGETPLHLA 193
Ank_2 pfam12796
Ankyrin repeats (3 copies);
117-205 1.17e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.40  E-value: 1.17e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450059   117 ANANDVETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHgADPNQQDGlGNTPLHLAACTNHVPVITTLLR 196
Cdd:pfam12796   5 AKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLLE 82


                  ....*....
gi 21450059   197 GGARVDALD 205
Cdd:pfam12796  83 KGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 116-215 3.11e-18

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 84.31  E-value: 3.11e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450059  116 SANANdVETVQQLLEDGADPCAADDKGRTALH-FA-SCNGNDQIVQLLLDHGADPNQQDGLGNTPLHLAA--CTNHVPVI 191
Cdd:PHA03095 162 SRNAN-VELLRLLIDAGADVYAVDDRFRSLLHhHLqSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMAtgSSCKRSLV 240

                         90       100
                 ....*....|....*....|....
gi 21450059  192 TTLLRGGARVDALDRAGRTPLHLA 215
Cdd:PHA03095 241 LPLLIAGISINARNRYGQTPLHYA 264
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 120-221 1.32e-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: 64.65  E-value: 1.32e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450059 120 NDVETVQQLLEDGADPCAAD------DKGRTAL-----H---FASCNGNDQIVQLLLDHGADPNQQDGLGNTPLH-LAAC 184
Cdd:cd22192 100 QNLNLVRELIARGADVVSPRatgtffRPGPKNLiyygeHplsFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHiLVLQ 179

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 21450059 185 TNHVPV------ITTLLRGG--ARVDAL-DRAGRTPLHLAKSKLNI 221
Cdd:cd22192 180 PNKTFAcqmydlILSYDKEDdlQPLDLVpNNQGLTPFKLAAKEGNI 225
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 141-169 5.31e-07

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: 45.27  E-value: 5.31e-07
                           10        20
                   ....*....|....*....|....*....
gi 21450059    141 KGRTALHFASCNGNDQIVQLLLDHGADPN 169
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 120-221 9.92e-07

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 50.08  E-value: 9.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450059   120 NDVETVQQLLEDGAD---PCAADD-----------KGRTALHFASCNGNDQIVQLLLDHGADPNQQDGLGNTPLHLAACT 185
Cdd:TIGR00870 139 QNYEIVKLLLERGASvpaRACGDFfvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVME 218

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 21450059   186 NHVPVITT---------LLRGGARVDA-------LDRAGRTPLHLAKSKLNI 221
Cdd:TIGR00870 219 NEFKAEYEelscqmynfALSLLDKLRDskeleviLNHQGLTPLKLAAKEGRI 270
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 153-299 1.56e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 43.32  E-value: 1.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450059  153 GNDQIVQLLLDHGADPNQQDGLGNTPLHLAACTNHVPVITTLLRGGARVDALDRAGRTPLHLAKSK-----LNILQE--- 224
Cdd:PLN03192 536 GNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAkhhkiFRILYHfas 615

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450059  225 -------GHSQCLEAVRLEVKqiihMLREYLeRLGRHEQRERLDDLcTRLQMTSTKEQVDEVTDLL---ASFTSLSL--Q 292
Cdd:PLN03192 616 isdphaaGDLLCTAAKRNDLT----AMKELL-KQGLNVDSEDHQGA-TALQVAMAEDHVDMVRLLImngADVDKANTddD 689


                 ....*..
gi 21450059  293 MQSMEKR 299
Cdd:PLN03192 690 FSPTELR 696
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
113-215 1.96e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 123.91  E-value: 1.96e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450059 113 LRDSANANDVETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQQDGLGNTPLHLAACTNHVPVIT 192
Cdd:COG0666  91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                        90       100
                ....*....|....*....|...
gi 21450059 193 TLLRGGARVDALDRAGRTPLHLA 215
Cdd:COG0666 171 LLLEAGADVNARDNDGETPLHLA 193
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
117-220 8.51e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 122.37  E-value: 8.51e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450059 117 ANANDVETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQQDGLGNTPLHLAACTNHVPVITTLLR 196
Cdd:COG0666 128 AYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLE 207

                        90       100
                ....*....|....*....|....
gi 21450059 197 GGARVDALDRAGRTPLHLAKSKLN 220
Cdd:COG0666 208 AGADVNAKDNDGKTALDLAAENGN 231
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
113-215 1.11e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 100.41  E-value: 1.11e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450059 113 LRDSANANDVETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQQDGLGNTPLHLAACTNHVPVIT 192
Cdd:COG0666  58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137

                        90       100
                ....*....|....*....|...
gi 21450059 193 TLLRGGARVDALDRAGRTPLHLA 215
Cdd:COG0666 138 LLLEAGADVNAQDNDGNTPLHLA 160
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
117-222 8.28e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 98.10  E-value: 8.28e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450059 117 ANANDVETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQQDGLGNTPLHLAACTNHVPVITTLLR 196
Cdd:COG0666 161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                        90       100
                ....*....|....*....|....*.
gi 21450059 197 GGARVDALDRAGRTPLHLAKSKLNIL 222
Cdd:COG0666 241 AGADLNAKDKDGLTALLLAAAAGAAL 266
Ank_2 pfam12796
Ankyrin repeats (3 copies);
117-205 1.17e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.40  E-value: 1.17e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450059   117 ANANDVETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHgADPNQQDGlGNTPLHLAACTNHVPVITTLLR 196
Cdd:pfam12796   5 AKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLLE 82


                  ....*....
gi 21450059   197 GGARVDALD 205
Cdd:pfam12796  83 KGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 116-215 3.11e-18

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 84.31  E-value: 3.11e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450059  116 SANANdVETVQQLLEDGADPCAADDKGRTALH-FA-SCNGNDQIVQLLLDHGADPNQQDGLGNTPLHLAA--CTNHVPVI 191
Cdd:PHA03095 162 SRNAN-VELLRLLIDAGADVYAVDDRFRSLLHhHLqSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMAtgSSCKRSLV 240

                         90       100
                 ....*....|....*....|....
gi 21450059  192 TTLLRGGARVDALDRAGRTPLHLA 215
Cdd:PHA03095 241 LPLLIAGISINARNRYGQTPLHYA 264
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 121-219 5.69e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 80.69  E-value: 5.69e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450059  121 DVETVQQLLEDGADPCAAD-DKGRTALHFASCNGNDQIVQLLLDHGADPNQQDGLGNTPLHLAACTNHVPVITTLLRGGA 199
Cdd:PHA02878 146 EAEITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225

                         90       100
                 ....*....|....*....|
gi 21450059  200 RVDALDRAGRTPLHLAKSKL 219
Cdd:PHA02878 226 STDARDKCGNTPLHISVGYC 245
PHA03095 PHA03095
ankyrin-like protein; Provisional
 98-243 1.35e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 79.68  E-value: 1.35e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450059   98 RRLGPTGKEVH--------ALKRLRDSANANDVETVQQLLEDGADPCAADDKGRTALHFASCNGND-QIVQLLLDHGADP 168
Cdd:PHA03095  31 RRLLAAGADVNfrgeygktPLHLYLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGADV 110

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21450059  169 NQQDGLGNTPLHlAACTN---HVPVITTLLRGGARVDALDRAGRTPLHlaksklnILQEGHSQCLEAVRLEVKQIIHM 243
Cdd:PHA03095 111 NAKDKVGRTPLH-VYLSGfniNPKVIRLLLRKGADVNALDLYGMTPLA-------VLLKSRNANVELLRLLIDAGADV 180
Ank_2 pfam12796
Ankyrin repeats (3 copies);
146-231 2.87e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.46  E-value: 2.87e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450059   146 LHFASCNGNDQIVQLLLDHGADPNQQDGLGNTPLHLAACTNHVPVITTLLRgGARVDALDRaGRTPLHLAksklniLQEG 225
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYA------ARSG 72


                  ....*.
gi 21450059   226 HSQCLE 231
Cdd:pfam12796  73 HLEIVK 78
PHA03095 PHA03095
ankyrin-like protein; Provisional
 110-221 1.82e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 73.14  E-value: 1.82e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450059  110 LKRLRDSANAnDVETVQQLLEDGADPCAADDKGRTALH-FASCNGND--QIVQLLLDHGADPNQQDGLGNTPLHLAACTN 186
Cdd:PHA03095  16 YDYLLNASNV-TVEEVRRLLAAGADVNFRGEYGKTPLHlYLHYSSEKvkDIVRLLLEAGADVNAPERCGFTPLHLYLYNA 94

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 21450059  187 HV-PVITTLLRGGARVDALDRAGRTPLHLAKSKLNI 221
Cdd:PHA03095  95 TTlDVIKLLIKAGADVNAKDKVGRTPLHVYLSGFNI 130
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
109-215 2.86e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 68.83  E-value: 2.86e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450059 109 ALKRLRDSANANDVETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQQDGLGNTPLHLAACTNHV 188
Cdd:COG0666  21 LALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDL 100

                        90       100
                ....*....|....*....|....*..
gi 21450059 189 PVITTLLRGGARVDALDRAGRTPLHLA 215
Cdd:COG0666 101 EIVKLLLEAGADVNARDKDGETPLHLA 127
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 123-215 4.11e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 69.22  E-value: 4.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450059  123 ETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQQDGLGNTPLHLAACTNHVPVITTLLRGGARVD 202
Cdd:PHA02874 105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184

                         90
                 ....*....|...
gi 21450059  203 ALDRAGRTPLHLA 215
Cdd:PHA02874 185 VKDNNGESPLHNA 197
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
117-212 1.22e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 66.90  E-value: 1.22e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450059 117 ANANDVETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQQDGLGNTPLHLAACTNHVPVITTLLR 196
Cdd:COG0666 194 AENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLL 273

                        90
                ....*....|....*.
gi 21450059 197 GGARVDALDRAGRTPL 212
Cdd:COG0666 274 ALLLLAAALLDLLTLL 289
PHA03095 PHA03095
ankyrin-like protein; Provisional
 125-215 1.34e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 67.74  E-value: 1.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450059  125 VQQLLEDGADPCAADDKGRTALH----FASCNgnDQIVQLLLDHGADPNQQDGLGNTPLHLAACTNHVPVITTLLRGGAR 200
Cdd:PHA03095 205 VRELIRAGCDPAATDMLGNTPLHsmatGSSCK--RSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGAD 282

                         90
                 ....*....|....*
gi 21450059  201 VDALDRAGRTPLHLA 215
Cdd:PHA03095 283 INAVSSDGNTPLSLM 297
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 116-215 1.41e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 67.78  E-value: 1.41e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450059  116 SANANDVETVQQLLEDGADPCAADDKGRTALHFASC-NGNDQIVQLLLDHGADPNQQDGLGNTPLHLAACTNHVPVITTL 194
Cdd:PHA02876 315 AKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTL 394

                         90       100
                 ....*....|....*....|.
gi 21450059  195 LRGGARVDALDRAGRTPLHLA 215
Cdd:PHA02876 395 LDYGADIEALSQKIGTALHFA 415
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 125-222 4.04e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 66.63  E-value: 4.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450059  125 VQQLLEDGADPCAADDKGRTALHFASCNGND-QIVQLLLDHGADPNQQDGLGNTPLHLAACTN-HVPVITTLLRGGARVD 202
Cdd:PHA02876 290 VPKLLERGADVNAKNIKGETPLYLMAKNGYDtENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVN 369

                         90       100
                 ....*....|....*....|
gi 21450059  203 ALDRAGRTPLHLAKSKLNIL 222
Cdd:PHA02876 370 ARDYCDKTPIHYAAVRNNVV 389
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 114-223 6.58e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 65.46  E-value: 6.58e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450059  114 RDSANANDVETvqqLLEDGADPCAADDKGRTALHFASCNG-----NDQIVQLLLDHGADPNQQDGLGNTPLHLAACT--N 186
Cdd:PHA03100  43 KEARNIDVVKI---LLDNGADINSSTKNNSTPLHYLSNIKynltdVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksN 119

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 21450059  187 HVPVITTLLRGGARVDALDRAGRTPLHLA----KSKLNILQ 223
Cdd:PHA03100 120 SYSIVEYLLDNGANVNIKNSDGENLLHLYlesnKIDLKILK 160
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 120-221 1.32e-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: 64.65  E-value: 1.32e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450059 120 NDVETVQQLLEDGADPCAAD------DKGRTAL-----H---FASCNGNDQIVQLLLDHGADPNQQDGLGNTPLH-LAAC 184
Cdd:cd22192 100 QNLNLVRELIARGADVVSPRatgtffRPGPKNLiyygeHplsFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHiLVLQ 179

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 21450059 185 TNHVPV------ITTLLRGG--ARVDAL-DRAGRTPLHLAKSKLNI 221
Cdd:cd22192 180 PNKTFAcqmydlILSYDKEDdlQPLDLVpNNQGLTPFKLAAKEGNI 225
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 117-196 1.47e-11

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 64.92  E-value: 1.47e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450059  117 ANANDVETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQQDGLGNTPLHLAACTNHVPVITTLLR 196
Cdd:PTZ00322  90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 110-215 1.54e-11

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 64.53  E-value: 1.54e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450059  110 LKRLRDSANANDVETVQQLLEDGADPCAADDKGRTALHFAScNGNDQIVQLLLDHGADPNQQDGLGNTPLHLAACTNHVP 189
Cdd:PTZ00322  51 LEALEATENKDATPDHNLTTEEVIDPVVAHMLTVELCQLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQ 129

                         90       100
                 ....*....|....*....|....*.
gi 21450059  190 VITTLLRGGARVDALDRAGRTPLHLA 215
Cdd:PTZ00322 130 VVRVLLEFGADPTLLDKDGKTPLELA 155
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 125-206 1.79e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 64.30  E-value: 1.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450059  125 VQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQQDGLGNTPLHLAACTNHVPVITTLLRGGARVDAL 204
Cdd:PHA03100 175 VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTI 254


                 ..
gi 21450059  205 DR 206
Cdd:PHA03100 255 IE 256
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 120-215 1.90e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 63.92  E-value: 1.90e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450059  120 NDVETVQQLLEDGADPCAADDKGRTALH-FASCNGND-QIVQLLLDHGADPNQQDGL----------------GNTPLHL 181
Cdd:PHA03100 119 NSYSIVEYLLDNGANVNIKNSDGENLLHlYLESNKIDlKILKLLIDKGVDINAKNRVnyllsygvpinikdvyGFTPLHY 198

                         90       100       110
                 ....*....|....*....|....*....|....
gi 21450059  182 AACTNHVPVITTLLRGGARVDALDRAGRTPLHLA 215
Cdd:PHA03100 199 AVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIA 232
PHA02946 PHA02946
ankyin-like protein; Provisional
 121-212 1.28e-10

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 61.61  E-value: 1.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450059  121 DVETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQQDGLGNTPLHLAACTNH--VPVITTLLRGG 198
Cdd:PHA02946  51 DERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYG 130

                         90
                 ....*....|....*
gi 21450059  199 ARV-DALDRAGRTPL 212
Cdd:PHA02946 131 AKInNSVDEEGCGPL 145
Ank_4 pfam13637
Ankyrin repeats (many copies);
142-195 1.37e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.74  E-value: 1.37e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 21450059   142 GRTALHFASCNGNDQIVQLLLDHGADPNQQDGLGNTPLHLAACTNHVPVITTLL 195
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 120-215 1.91e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 61.13  E-value: 1.91e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450059  120 NDVETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQQDGLGNTPLHLAACTNHVPVITTLLRGGA 199
Cdd:PHA02874 135 GDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGN 214

                         90
                 ....*....|....*.
gi 21450059  200 RVDALDRAGRTPLHLA 215
Cdd:PHA02874 215 HIMNKCKNGFTPLHNA 230
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 116-222 5.45e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 60.08  E-value: 5.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450059  116 SANANDVETVQQLLEDGADPCAADDKGRTALHFASCNGNDQI-VQLLLDHGADPNQQDGLGNTPLHLAACTNHVP-VITT 193
Cdd:PHA02876 382 AAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVNSKNKDLSTPLHYACKKNCKLdVIEM 461

                         90       100       110
                 ....*....|....*....|....*....|..
gi 21450059  194 LLRGGARVDALDRAGRTPLHLA---KSKLNIL 222
Cdd:PHA02876 462 LLDNGADVNAINIQNQYPLLIAleyHGIVNIL 493
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 106-201 7.05e-10

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 59.64  E-value: 7.05e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450059 106 EVHAL--KRLRDS-----ANANDVETVQQLLE-DGADPCAADDKGRTALHFASCNGNDQIVQLLLDhgADP---NQ---- 170
Cdd:cd22192   7 ELHLLqqKRISESplllaAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPelvNEpmts 84

                        90       100       110
                ....*....|....*....|....*....|.
gi 21450059 171 QDGLGNTPLHLAACTNHVPVITTLLRGGARV 201
Cdd:cd22192  85 DLYQGETALHIAVVNQNLNLVRELIARGADV 115
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 113-221 9.83e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 58.85  E-value: 9.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450059  113 LRDSANANDVETVQQLLEDGAdpcAADD----KGRTALHFASCNGNDQIVQLLLDHGADPNQQDGLGNTPLHLAACTNHV 188
Cdd:PHA02875  72 LHDAVEEGDVKAVEELLDLGK---FADDvfykDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI 148

                         90       100       110
                 ....*....|....*....|....*....|...
gi 21450059  189 PVITTLLRGGARVDALDRAGRTPLHLAKSKLNI 221
Cdd:PHA02875 149 KGIELLIDHKACLDIEDCCGCTPLIIAMAKGDI 181
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 125-226 1.23e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 59.11  E-value: 1.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450059  125 VQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQQDGLGNTPL----------------HLAA----- 183
Cdd:PLN03192 541 LEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnaisakhhkifrilyHFASisdph 620

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 21450059  184 ------CT----NHVPVITTLLRGGARVDALDRAGRTPLHLAksklniLQEGH 226
Cdd:PLN03192 621 aagdllCTaakrNDLTAMKELLKQGLNVDSEDHQGATALQVA------MAEDH 667
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 141-213 5.99e-09

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: 56.74  E-value: 5.99e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450059 141 KGRTALHFASCNGNDQIVQLLLDHGADPN------------QQDG--LGNTPLHLAACTNHVPVITTLLRG---GARVDA 203
Cdd:cd22196  93 KGQTALHIAIERRNMHLVELLVQNGADVHarasgeffkkkkGGPGfyFGELPLSLAACTNQLDIVKFLLENphsPADISA 172

                        90
                ....*....|
gi 21450059 204 LDRAGRTPLH 213
Cdd:cd22196 173 RDSMGNTVLH 182
Ank_5 pfam13857
Ankyrin repeats (many copies);
128-182 2.46e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 49.65  E-value: 2.46e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 21450059   128 LLEDG-ADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQQDGLGNTPLHLA 182
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 108-220 3.36e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 54.12  E-value: 3.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450059  108 HALKRLRDSANANDVETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQQD-GLGNTPLHLAACTN 186
Cdd:PHA02878 100 YTLVAIKDAFNNRNVEIFKIILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDrHKGNTALHYATENK 179

                         90       100       110
                 ....*....|....*....|....*....|....
gi 21450059  187 HVPVITTLLRGGARVDALDRAGRTPLHLAKSKLN 220
Cdd:PHA02878 180 DQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYN 213
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 121-208 4.23e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 53.84  E-value: 4.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450059  121 DVETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQQDGLGNTPLHLAACTNHVPVITTLLRGGAR 200
Cdd:PHA02875 114 KLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGAN 193


                 ....*...
gi 21450059  201 VDALDRAG 208
Cdd:PHA02875 194 IDYFGKNG 201
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 125-221 4.73e-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: 54.12  E-value: 4.73e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450059 125 VQQLLEDGAD-------------PCAADDKGRTALHFASCNGNDQIVQLLLDHGADP---NQQDGLGNTPLH-LAACTNH 187
Cdd:cd21882  89 VRLLVENGADvsaratgrffrksPGNLFYFGELPLSLAACTNQEEIVRLLLENGAQPaalEAQDSLGNTVLHaLVLQADN 168

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 21450059 188 VPVITT--------LLRGGARVDAL-------DRAGRTPLHLAKSKLNI 221
Cdd:cd21882 169 TPENSAfvcqmynlLLSYGAHLDPTqqleeipNHQGLTPLKLAAVEGKI 217
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 121-212 7.59e-08

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 53.38  E-value: 7.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450059  121 DVETVQQLLEDGADPCAADDKGRTALH--FASCNGNDQIVQLLLDHGADPNQQDGLGNTPLH-----------LAACTNH 187
Cdd:PHA02716 296 DISVVYSFLQPGVKLHYKDSAGRTCLHqyILRHNISTDIIKLLHEYGNDLNEPDNIGNTVLHtylsmlsvvniLDPETDN 375

                         90       100
                 ....*....|....*....|....*...
gi 21450059  188 ---VPVITTLLRGGARVDALDRAGRTPL 212
Cdd:PHA02716 376 dirLDVIQCLISLGADITAVNCLGYTPL 403
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 121-217 8.19e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 53.14  E-value: 8.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450059  121 DVETVQQLLEDGADPCAADDKGRTALHFASCNGN-DQIVQLLLDHGADPNQQDGLGNTPLHLAACTNH-VPVITTLLRGG 198
Cdd:PHA02876 252 DLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLG 331

                         90
                 ....*....|....*....
gi 21450059  199 ARVDALDRAGRTPLHLAKS 217
Cdd:PHA02876 332 ADVNAADRLYITPLHQAST 350
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 120-215 1.42e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 52.27  E-value: 1.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450059  120 NDVETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQQDGLGNTPLHLAACTNHVPVitTLLRGGA 199
Cdd:PHA02874 168 NFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAI--ELLINNA 245

                         90
                 ....*....|....*.
gi 21450059  200 RVDALDRAGRTPLHLA 215
Cdd:PHA02874 246 SINDQDIDGSTPLHHA 261
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 141-213 2.26e-07

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 51.80  E-value: 2.26e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450059 141 KGRTALHFASCNGNDQIVQLLLDHGAD-------------PNQQDGLGNTPLHLAACTNHVPVITTLLRGGARVDAL--- 204
Cdd:cd21882  72 QGQTALHIAIENRNLNLVRLLVENGADvsaratgrffrksPGNLFYFGELPLSLAACTNQEEIVRLLLENGAQPAALeaq 151


                ....*....
gi 21450059 205 DRAGRTPLH 213
Cdd:cd21882 152 DSLGNTVLH 160
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 101-213 2.29e-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: 51.78  E-value: 2.29e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450059 101 GPTGKE--VHALKRLRDSANAndveTVQQLLEDGADP----------CAAD-DKGRTALHFASCNGNDQIVQLLLDHGAD 167
Cdd:cd22197  44 GSTGKTclMKAVLNLQDGVNA----CIMPLLEIDKDSgnpkplvnaqCTDEyYRGHSALHIAIEKRSLQCVKLLVENGAD 119

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21450059 168 PN---------QQDG----LGNTPLHLAACTNHVPVITTLLRGG---ARVDALDRAGRTPLH 213
Cdd:cd22197 120 VHaracgrffqKKQGtcfyFGELPLSLAACTKQWDVVNYLLENPhqpASLQAQDSLGNTVLH 181
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 141-172 2.60e-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: 46.13  E-value: 2.60e-07
                          10        20        30
                  ....*....|....*....|....*....|...
gi 21450059   141 KGRTALHFASC-NGNDQIVQLLLDHGADPNQQD 172
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
Ank_4 pfam13637
Ankyrin repeats (many copies);
117-162 2.80e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.50  E-value: 2.80e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 21450059   117 ANANDVETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLL 162
Cdd:pfam13637   9 AASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 118-213 2.89e-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: 51.68  E-value: 2.89e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450059 118 NANDVETVQQLL----EDG-------ADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPN------------QQDG- 173
Cdd:cd22194 106 NENTKEIVRILLafaeENGildrfinAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNahakgvffnpkyKHEGf 185

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 21450059 174 -LGNTPLHLAACTNHVPVITTLL-RGGARVDALDRAGRTPLH 213
Cdd:cd22194 186 yFGETPLALAACTNQPEIVQLLMeKESTDITSQDSRGNTVLH 227
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 159-229 2.90e-07

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 49.10  E-value: 2.90e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21450059  159 QLLLDHGADPNQQDGL-GNTPLHLAACTNHVPVITTLLRG-GARVDALDRAGRTPLHLAKSK-----LNILQEGHSQC 229
Cdd:PHA02736  75 KLLMEWGADINGKERVfGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERhdakmMNILRAKGAQC 152
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 125-215 2.93e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 51.42  E-value: 2.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450059  125 VQQLLEDGADPCAADDKGRTALHFASCNGND-QIVQLLLDHGADPNQQDG-LGNTPLHLAActnHVP-VITTLLRGGARV 201
Cdd:PHA02878 217 VHILLENGASTDARDKCGNTPLHISVGYCKDyDILKLLLEHGVDVNAKSYiLGLTALHSSI---KSErKLKLLLEYGADI 293

                         90
                 ....*....|....
gi 21450059  202 DALDRAGRTPLHLA 215
Cdd:PHA02878 294 NSLNSYKLTPLSSA 307
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 141-213 4.44e-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: 50.95  E-value: 4.44e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450059 141 KGRTALHFASCNGNDQIVQLLLDHGAD-----------PNQQDG---LGNTPLHLAACTNHVPVITTLLRGG---ARVDA 203
Cdd:cd22193  75 EGQTALHIAIERRQGDIVALLVENGADvhahakgrffqPKYQGEgfyFGELPLSLAACTNQPDIVQYLLENEhqpADIEA 154

                        90
                ....*....|
gi 21450059 204 LDRAGRTPLH 213
Cdd:cd22193 155 QDSRGNTVLH 164
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 141-169 5.31e-07

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: 45.27  E-value: 5.31e-07
                           10        20
                   ....*....|....*....|....*....
gi 21450059    141 KGRTALHFASCNGNDQIVQLLLDHGADPN 169
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 105-205 8.58e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 50.06  E-value: 8.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450059  105 KEVHALKRLRDSANANDVETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPN--QQDGLgnTPLHLA 182
Cdd:PHA02876 141 ESIEYMKLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNiiALDDL--SVLECA 218

                         90       100
                 ....*....|....*....|...
gi 21450059  183 ACTNHVPVITTLLRGGARVDALD 205
Cdd:PHA02876 219 VDSKNIDTIKAIIDNRSNINKND 241
PHA03095 PHA03095
ankyrin-like protein; Provisional
 125-207 9.49e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 49.64  E-value: 9.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450059  125 VQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQQDGLGNTPLHLAACTNHVPVITTLLRGGARVDAL 204
Cdd:PHA03095 240 VLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETV 319


                 ...
gi 21450059  205 DRA 207
Cdd:PHA03095 320 AAT 322
Ank_5 pfam13857
Ankyrin repeats (many copies);
161-215 9.66e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.03  E-value: 9.66e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 21450059   161 LLDHG-ADPNQQDGLGNTPLHLAACTNHVPVITTLLRGGARVDALDRAGRTPLHLA 215
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 120-221 9.92e-07

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 50.08  E-value: 9.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450059   120 NDVETVQQLLEDGAD---PCAADD-----------KGRTALHFASCNGNDQIVQLLLDHGADPNQQDGLGNTPLHLAACT 185
Cdd:TIGR00870 139 QNYEIVKLLLERGASvpaRACGDFfvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVME 218

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 21450059   186 NHVPVITT---------LLRGGARVDA-------LDRAGRTPLHLAKSKLNI 221
Cdd:TIGR00870 219 NEFKAEYEelscqmynfALSLLDKLRDskeleviLNHQGLTPLKLAAKEGRI 270
PHA02946 PHA02946
ankyin-like protein; Provisional
 154-213 1.64e-06

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 48.90  E-value: 1.64e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450059  154 NDQIVQLLLDHGADPNQQDGLGNTPLHLAACTNHVPVITTLLRGGARVDALDRAGRTPLH 213
Cdd:PHA02946  51 DERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLY 110
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 141-216 2.16e-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: 2.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450059   141 KGRTALHFASCNGNDQIVQLLLDHGADPN------------QQDGL--GNTPLHLAACTNHVPVITTLLRGGARVDALDR 206
Cdd:TIGR00870 127 PGITALHLAAHRQNYEIVKLLLERGASVParacgdffvksqGVDSFyhGESPLNAAACLGSPSIVALLSEDPADILTADS 206

                          90
                  ....*....|
gi 21450059   207 AGRTPLHLAK 216
Cdd:TIGR00870 207 LGNTLLHLLV 216
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 141-169 1.15e-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: 41.47  E-value: 1.15e-05
                          10        20
                  ....*....|....*....|....*....
gi 21450059   141 KGRTALHFASCNGNDQIVQLLLDHGADPN 169
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
Ank_4 pfam13637
Ankyrin repeats (many copies);
175-231 3.28e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.72  E-value: 3.28e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 21450059   175 GNTPLHLAACTNHVPVITTLLRGGARVDALDRAGRTPLHLAksklniLQEGHSQCLE 231
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFA------ASNGNVEVLK 51
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 115-213 4.67e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 43.65  E-value: 4.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450059  115 DSANANdVETVQQLLEDGAD-PCAADDKGRTALH-FASCNGN--DQIVQLLLDHGADPNQQDGLGNTPLH--LAACTNHV 188
Cdd:PHA02859  60 EKDKVN-VEILKFLIENGADvNFKTRDNNLSALHhYLSFNKNvePEILKILIDSGSSITEEDEDGKNLLHmyMCNFNVRI 138

                         90       100
                 ....*....|....*....|....*
gi 21450059  189 PVITTLLRGGARVDALDRAGRTPLH 213
Cdd:PHA02859 139 NVIKLLIDSGVSFLNKDFDNNNILY 163
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 113-220 9.14e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 43.80  E-value: 9.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450059  113 LRDSANANDVETVQQLLEDGADPCAADDKGRTALHFASCNgNDQIVQLLLDHgADPNQQDGLGNTPLHLA---ACTnhVP 189
Cdd:PHA02874 194 LHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIH-NRSAIELLINN-ASINDQDIDGSTPLHHAinpPCD--ID 269

                         90       100       110
                 ....*....|....*....|....*....|.
gi 21450059  190 VITTLLRGGARVDALDRAGRTPLHLAKSKLN 220
Cdd:PHA02874 270 IIDILLYHKADISIKDNKGENPIDTAFKYIN 300
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 175-206 1.09e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.81  E-value: 1.09e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 21450059   175 GNTPLHLAAC-TNHVPVITTLLRGGARVDALDR 206
Cdd:pfam00023   2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 153-299 1.56e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 43.32  E-value: 1.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450059  153 GNDQIVQLLLDHGADPNQQDGLGNTPLHLAACTNHVPVITTLLRGGARVDALDRAGRTPLHLAKSK-----LNILQE--- 224
Cdd:PLN03192 536 GNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAkhhkiFRILYHfas 615

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450059  225 -------GHSQCLEAVRLEVKqiihMLREYLeRLGRHEQRERLDDLcTRLQMTSTKEQVDEVTDLL---ASFTSLSL--Q 292
Cdd:PLN03192 616 isdphaaGDLLCTAAKRNDLT----AMKELL-KQGLNVDSEDHQGA-TALQVAMAEDHVDMVRLLImngADVDKANTddD 689


                 ....*..
gi 21450059  293 MQSMEKR 299
Cdd:PLN03192 690 FSPTELR 696
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 113-215 2.27e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 42.26  E-value: 2.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450059  113 LRDSANANDVETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADP-----------------------N 169
Cdd:PHA02874  39 LIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTsilpipciekdmiktildcgidvN 118

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 21450059  170 QQDGLGNTPLHLAACTNHVPVITTLLRGGARVDALDRAGRTPLHLA 215
Cdd:PHA02874 119 IKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIA 164
TRPV4 cd22195
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed ...
 141-213 2.69e-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: 42.53  E-value: 2.69e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450059 141 KGRTALHFASCNGNDQIVQLLLDHGAD-----------PNQQDG---LGNTPLHLAACTNHVPVITTLLRGGARVDAL-- 204
Cdd:cd22195 136 RGQTALHIAIERRCKHYVELLVEKGADvhaqargrffqPKDEGGyfyFGELPLSLAACTNQPDIVHYLTENAHKKADLrr 215

                        90
                ....*....|
gi 21450059 205 -DRAGRTPLH 213
Cdd:cd22195 216 qDSRGNTVLH 225
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 115-215 4.80e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 41.52  E-value: 4.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450059  115 DSANANDVETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQQDGLGNTPLHLAACTNHVPVITTL 194
Cdd:PHA02875   8 DAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEEL 87

                         90       100
                 ....*....|....*....|..
gi 21450059  195 LRGGARV-DALDRAGRTPLHLA 215
Cdd:PHA02875  88 LDLGKFAdDVFYKDGMTPLHLA 109
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 116-167 5.82e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 41.19  E-value: 5.82e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 21450059  116 SANANDVETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGAD 167
Cdd:PHA03100 199 AVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 175-203 6.98e-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: 36.41  E-value: 6.98e-04
                           10        20
                   ....*....|....*....|....*....
gi 21450059    175 GNTPLHLAACTNHVPVITTLLRGGARVDA 203
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02946 PHA02946
ankyin-like protein; Provisional
 97-213 9.11e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 40.42  E-value: 9.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450059   97 HRRLGPTGKEVHALKRLRDSANANDVETVQQLLEDGADPCAADDKGRTALHFASCNGNDQI--VQLLLDHGADPNQQ-DG 173
Cdd:PHA02946  60 HRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIerINLLVQYGAKINNSvDE 139

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 21450059  174 LGNTPlhLAACTNHVP-VITTLLRGGARVDALDRAGRTPLH 213
Cdd:PHA02946 140 EGCGP--LLACTDPSErVFKKIMSIGFEARIVDKFGKNHIH 178
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 122-164 1.19e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 40.27  E-value: 1.19e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 21450059  122 VETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDH 164
Cdd:PTZ00322 128 VQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PHA02791 PHA02791
ankyrin-like protein; Provisional
 113-162 2.91e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 38.48  E-value: 2.91e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 21450059  113 LRDSANANDVETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLL 162
Cdd:PHA02791  65 LHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGNMQTVKLFV 114
PHA02791 PHA02791
ankyrin-like protein; Provisional
 134-239 5.27e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 37.71  E-value: 5.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450059  134 DPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQQDglGNTPLHLAACTNHVPVITTLLRGGARVDALDRAGRTPLH 213
Cdd:PHA02791  22 DAFKADVHGHSALYYAIADNNVRLVCTLLNAGALKNLLE--NEFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALY 99

                         90       100
                 ....*....|....*....|....*.
gi 21450059  214 LAKSKLNilqeghsqcLEAVRLEVKQ 239
Cdd:PHA02791 100 YAVDSGN---------MQTVKLFVKK 116
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 157-221 5.98e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 38.12  E-value: 5.98e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21450059  157 IVQLLLDHGADPNQQDGLGNTPLHLAACTNHVPVITTLLRGGARVDALDRAGRTPLHLAKSKLNI 221
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNI 224
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 121-182 6.42e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 37.94  E-value: 6.42e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21450059  121 DVETVQQLLEDGADPCAADD-KGRTALHFAScnGNDQIVQLLLDHGADPNQQDGLGNTPLHLA 182
Cdd:PHA02878 247 DYDILKLLLEHGVDVNAKSYiLGLTALHSSI--KSERKLKLLLEYGADINSLNSYKLTPLSSA 307
PHA02798 PHA02798
ankyrin-like protein; Provisional
 122-235 9.19e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 37.51  E-value: 9.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450059  122 VETVQQLLEDGADPCAADDKGRTAL-----HFASCNGNDQIVQLLLDHGADPNQQDGLGNTPLHLA---ACTNHVPVITT 193
Cdd:PHA02798  51 TDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLlsnGYINNLEILLF 130

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 21450059  194 LLRGGARVDALDRAGRTPLHLaksklnILQEGHSQCLEAVRL 235
Cdd:PHA02798 131 MIENGADTTLLDKDGFTMLQV------YLQSNHHIDIEIIKL 166
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 116-167 1.00e-02

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 37.54  E-value: 1.00e-02
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 21450059  116 SANANDVETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGAD 167
Cdd:PLN03192 629 AAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGAD 680
 
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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