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Conserved domains on  [gi|149068458|gb|EDM18010|]
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integrin linked kinase, isoform CRA_d [Rattus norvegicus]

Protein Classification

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

ankyrin repeat domain-containing protein; ANK proteins mediate specific protein-protein interactions without necessarily recognizing specific primary sequences which allows for one ankyrin repeat domain to recognize and bind to a variety of intracellular substrates and may be involved in a wide array of functions

Gene Ontology:  GO:0005515
PubMed:  17176038
SCOP:  4000366

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
8-117 9.01e-35

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 123.14  E-value: 9.01e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068458   8 CREGNAVAVRLWLDNtENDLNQGDDHGFSPLHWACREGRSAVVEMLIMRGARINVMNRGDDTPLHLAASHGHRDIVQKLL 87
Cdd:COG0666   95 ARNGDLEIVKLLLEA-GADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLL 173

                         90       100       110
                 ....*....|....*....|....*....|
gi 149068458  88 QYKADINAVNEHGNVPLHYACFWGQDQVAE 117
Cdd:COG0666  174 EAGADVNARDNDGETPLHLAAENGHLEIVK 203
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
8-117 9.01e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 123.14  E-value: 9.01e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068458   8 CREGNAVAVRLWLDNtENDLNQGDDHGFSPLHWACREGRSAVVEMLIMRGARINVMNRGDDTPLHLAASHGHRDIVQKLL 87
Cdd:COG0666   95 ARNGDLEIVKLLLEA-GADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLL 173

                         90       100       110
                 ....*....|....*....|....*....|
gi 149068458  88 QYKADINAVNEHGNVPLHYACFWGQDQVAE 117
Cdd:COG0666  174 EAGADVNARDNDGETPLHLAAENGHLEIVK 203
Ank_2 pfam12796
Ankyrin repeats (3 copies);
38-117 9.31e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.00  E-value: 9.31e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068458   38 LHWACREGRSAVVEMLIMRGARINVMNRGDDTPLHLAASHGHRDIVQKLLQYkADINAVNeHGNVPLHYACFWGQDQVAE 117
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 26-107 3.04e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 78.00  E-value: 3.04e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068458  26 DLNQGDDH-GFSPLHWACREGRSAVVEMLIMRGARINVMNRGDDTPLHLAASHGHRDIVQKLLQYKADINAVNEHGNVPL 104
Cdd:PHA02878 159 DINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPL 238


                 ...
gi 149068458 105 HYA 107
Cdd:PHA02878 239 HIS 241
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 67-95 1.43e-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: 45.66  E-value: 1.43e-07
                           10        20
                   ....*....|....*....|....*....
gi 149068458    67 DDTPLHLAASHGHRDIVQKLLQYKADINA 95
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 34-105 4.28e-05

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 42.69  E-value: 4.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068458  34 GFSPLHWACREGRSAVVEMLIMRGARIN---------VMNRGD-----DTPLHLAASHGHRDIVQKLLQYKADINAVNEH 99
Cdd:cd22192   89 GETALHIAVVNQNLNLVRELIARGADVVspratgtffRPGPKNliyygEHPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168


                 ....*.
gi 149068458 100 GNVPLH 105
Cdd:cd22192  169 GNTVLH 174
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 33-105 2.08e-04

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: 40.83  E-value: 2.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068458   33 HGFSPLHWACREGRSAVVEMLIMRGARINVMNRGDD--------------TPLHLAASHGHRDIVQKLLQYKADINAVNE 98
Cdd:TIGR00870 127 PGITALHLAAHRQNYEIVKLLLERGASVPARACGDFfvksqgvdsfyhgeSPLNAAACLGSPSIVALLSEDPADILTADS 206


                  ....*..
gi 149068458   99 HGNVPLH 105
Cdd:TIGR00870 207 LGNTLLH 213
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
8-117 9.01e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 123.14  E-value: 9.01e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068458   8 CREGNAVAVRLWLDNtENDLNQGDDHGFSPLHWACREGRSAVVEMLIMRGARINVMNRGDDTPLHLAASHGHRDIVQKLL 87
Cdd:COG0666   95 ARNGDLEIVKLLLEA-GADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLL 173

                         90       100       110
                 ....*....|....*....|....*....|
gi 149068458  88 QYKADINAVNEHGNVPLHYACFWGQDQVAE 117
Cdd:COG0666  174 EAGADVNARDNDGETPLHLAAENGHLEIVK 203
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
8-117 1.47e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 117.36  E-value: 1.47e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068458   8 CREGNAVAVRLWLDNtENDLNQGDDHGFSPLHWACREGRSAVVEMLIMRGARINVMNRGDDTPLHLAASHGHRDIVQKLL 87
Cdd:COG0666  128 AYNGNLEIVKLLLEA-GADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLL 206

                         90       100       110
                 ....*....|....*....|....*....|
gi 149068458  88 QYKADINAVNEHGNVPLHYACFWGQDQVAE 117
Cdd:COG0666  207 EAGADVNAKDNDGKTALDLAAENGNLEIVK 236
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
10-117 5.44e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 108.12  E-value: 5.44e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068458  10 EGNAVAVRLWLDNTENDLNQGDDHGFSPLHWACREGRSAVVEMLIMRGARINVMNRGDDTPLHLAASHGHRDIVQKLLQY 89
Cdd:COG0666   63 LAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA 142

                         90       100
                 ....*....|....*....|....*...
gi 149068458  90 KADINAVNEHGNVPLHYACFWGQDQVAE 117
Cdd:COG0666  143 GADVNAQDNDGNTPLHLAAANGNLEIVK 170
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
8-117 2.55e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 87.70  E-value: 2.55e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068458   8 CREGNAVAVRLWLDNTEnDLNQGDDHGFSPLHWACREGRSAVVEMLIMRGARINVMNRGDDTPLHLAASHGHRDIVQKLL 87
Cdd:COG0666  161 AANGNLEIVKLLLEAGA-DVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239

                         90       100       110
                 ....*....|....*....|....*....|
gi 149068458  88 QYKADINAVNEHGNVPLHYACFWGQDQVAE 117
Cdd:COG0666  240 EAGADLNAKDKDGLTALLLAAAAGAALIVK 269
Ank_2 pfam12796
Ankyrin repeats (3 copies);
38-117 9.31e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.00  E-value: 9.31e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068458   38 LHWACREGRSAVVEMLIMRGARINVMNRGDDTPLHLAASHGHRDIVQKLLQYkADINAVNeHGNVPLHYACFWGQDQVAE 117
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
Ank_2 pfam12796
Ankyrin repeats (3 copies);
8-97 1.43e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.92  E-value: 1.43e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068458    8 CREGNAVAVRLWLDNtENDLNQGDDHGFSPLHWACREGRSAVVEMLImRGARINVMNRGDdTPLHLAASHGHRDIVQKLL 87
Cdd:pfam12796   5 AKNGNLELVKLLLEN-GADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDNGR-TALHYAARSGHLEIVKLLL 81

                          90
                  ....*....|
gi 149068458   88 QYKADINAVN 97
Cdd:pfam12796  82 EKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-117 3.87e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 79.23  E-value: 3.87e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068458   1 MDDIFTQCREGNAVAVRLWLDNTENDLNQGDDHGFSPLHWACREGRSAVVEMLIMRGARINVMNRGDDTPLHLAASHGHR 80
Cdd:COG0666   21 LALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDL 100

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 149068458  81 DIVQKLLQYKADINAVNEHGNVPLHYACFWGQDQVAE 117
Cdd:COG0666  101 EIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 26-107 3.04e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 78.00  E-value: 3.04e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068458  26 DLNQGDDH-GFSPLHWACREGRSAVVEMLIMRGARINVMNRGDDTPLHLAASHGHRDIVQKLLQYKADINAVNEHGNVPL 104
Cdd:PHA02878 159 DINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPL 238


                 ...
gi 149068458 105 HYA 107
Cdd:PHA02878 239 HIS 241
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 26-108 4.95e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 62.76  E-value: 4.95e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068458  26 DLNQGDDHGFSPLHWA--CREGRSAVVEMLIMRGARINVMNRGD----------------DTPLHLAASHGHRDIVQKLL 87
Cdd:PHA03100 133 NVNIKNSDGENLLHLYleSNKIDLKILKLLIDKGVDINAKNRVNyllsygvpinikdvygFTPLHYAVYNNNPEFVKYLL 212

                         90       100
                 ....*....|....*....|.
gi 149068458  88 QYKADINAVNEHGNVPLHYAC 108
Cdd:PHA03100 213 DLGANPNLVNKYGDTPLHIAI 233
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 11-89 5.59e-12

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 62.99  E-value: 5.59e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 149068458  11 GNAVAVRLWLDNTEnDLNQGDDHGFSPLHWACREGRSAVVEMLIMRGARINVMNRGDDTPLHLAASHGHRDIVQKLLQY 89
Cdd:PTZ00322  93 GDAVGARILLTGGA-DPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
Ank_4 pfam13637
Ankyrin repeats (many copies);
36-87 3.54e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.36  E-value: 3.54e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 149068458   36 SPLHWACREGRSAVVEMLIMRGARINVMNRGDDTPLHLAASHGHRDIVQKLL 87
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 16-105 1.19e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 58.88  E-value: 1.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068458  16 VRLWLDNTEnDLNQGDDHGFSPLH-WACREGRSAVVEMLIMRGARINVMNRGDDTPLH--LAASHGHRDIVQKLLQYKAD 92
Cdd:PHA03095  66 VRLLLEAGA-DVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGAD 144

                         90
                 ....*....|...
gi 149068458  93 INAVNEHGNVPLH 105
Cdd:PHA03095 145 VNALDLYGMTPLA 157
Ank_4 pfam13637
Ankyrin repeats (many copies);
69-117 2.67e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.05  E-value: 2.67e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 149068458   69 TPLHLAASHGHRDIVQKLLQYKADINAVNEHGNVPLHYACFWGQDQVAE 117
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLK 51
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 26-99 2.72e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 57.75  E-value: 2.72e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 149068458  26 DLNQGDDHGFSPLHWACREGRSAVVEMLIMRGARINVMNRGDDTPLHLAASHGHRDIVQKLLQYKADINAVNEH 99
Cdd:PHA03100 184 PINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
PHA03095 PHA03095
ankyrin-like protein; Provisional
 3-107 2.89e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 57.73  E-value: 2.89e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068458   3 DIFTQCREGNAVAVRLWLDNTENDLNQgDDHGFSPLHWACR--EGRSAVVEMLIMRGARINVMNRGDDTPLHLAASHG-- 78
Cdd:PHA03095 157 AVLLKSRNANVELLRLLIDAGADVYAV-DDRFRSLLHHHLQsfKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSsc 235

                         90       100
                 ....*....|....*....|....*....
gi 149068458  79 HRDIVQKLLQYKADINAVNEHGNVPLHYA 107
Cdd:PHA03095 236 KRSLVLPLLIAGISINARNRYGQTPLHYA 264
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 26-109 3.02e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 57.75  E-value: 3.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068458  26 DLNQGDDHGFSPLHWACRE--GRSAVVEMLIMRGARINVMNRGDDTPLHLAASHGHRD--IVQKLLQYKADINA------ 95
Cdd:PHA03100  98 NVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDINAknrvny 177

                         90       100
                 ....*....|....*....|....
gi 149068458  96 ----------VNEHGNVPLHYACF 109
Cdd:PHA03100 178 llsygvpiniKDVYGFTPLHYAVY 201
Ank_5 pfam13857
Ankyrin repeats (many copies);
56-107 3.65e-10

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 53.12  E-value: 3.65e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 149068458   56 RGARINVMNRGDDTPLHLAASHGHRDIVQKLLQYKADINAVNEHGNVPLHYA 107
Cdd:pfam13857   5 GPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 26-111 8.42e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 56.51  E-value: 8.42e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068458  26 DLNQGDDHGFSPLHWACREGRSAVVEMLIMRGARINVMNRGDDTPLHLAASHGHRDIVQKLLQYKADINAVNEHGNVPLH 105
Cdd:PHA02874 116 DVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLH 195


                 ....*.
gi 149068458 106 YACFWG 111
Cdd:PHA02874 196 NAAEYG 201
PHA03095 PHA03095
ankyrin-like protein; Provisional
 26-105 1.63e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 55.42  E-value: 1.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068458  26 DLNQGDDHGFSPLHWACR---EGRSAVVEMLIMRGARINVMNRGDDTPLHLAASHGHR-DIVQKLLQYKADINAVNEHGN 101
Cdd:PHA03095  39 DVNFRGEYGKTPLHLYLHyssEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGADVNAKDKVGR 118


                 ....
gi 149068458 102 VPLH 105
Cdd:PHA03095 119 TPLH 122
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 26-115 3.59e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 54.58  E-value: 3.59e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068458  26 DLNQGDDHGFSPLHWACREGRSAVVEMLIMRGARINVMNRGDDTPLHLAASHGHRDIVQKLLQYKADINAVNEHGNVPLH 105
Cdd:PHA02874 149 DVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLH 228

                         90
                 ....*....|
gi 149068458 106 YACFWGQDQV 115
Cdd:PHA02874 229 NAIIHNRSAI 238
Ank_5 pfam13857
Ankyrin repeats (many copies);
20-74 3.91e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.04  E-value: 3.91e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 149068458   20 LDNTENDLNQGDDHGFSPLHWACREGRSAVVEMLIMRGARINVMNRGDDTPLHLA 74
Cdd:pfam13857   2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 26-107 5.50e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 53.90  E-value: 5.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068458  26 DLNQGDDHGFSPLHWACREGRSA-----VVEMLIMRGARINVMNRGDDTPLHLAASH--GHRDIVQKLLQYKADINAVNE 98
Cdd:PHA03100  60 DINSSTKNNSTPLHYLSNIKYNLtdvkeIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNS 139


                 ....*....
gi 149068458  99 HGNVPLHYA 107
Cdd:PHA03100 140 DGENLLHLY 148
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 11-107 8.30e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.43  E-value: 8.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068458  11 GNAVAVRLWLDNTENDLNQGDDhGFSPLHWACREGRSaVVEMLImRGARINVMNRGDDTPLHLAASHG-HRDIVQKLLQY 89
Cdd:PHA02874 201 GDYACIKLLIDHGNHIMNKCKN-GFTPLHNAIIHNRS-AIELLI-NNASINDQDIDGSTPLHHAINPPcDIDIIDILLYH 277

                         90
                 ....*....|....*...
gi 149068458  90 KADINAVNEHGNVPLHYA 107
Cdd:PHA02874 278 KADISIKDNKGENPIDTA 295
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 25-107 8.54e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 53.35  E-value: 8.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068458  25 NDLNQGDDhgfSPLHWACREGRSAVVEMLIMRGARINVMNRGDDTPLHLAAS-------------HG------------- 78
Cdd:PHA02878 195 NIPDKTNN---SPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGyckdydilkllleHGvdvnaksyilglt 271

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 149068458  79 -------HRDIVQKLLQYKADINAVNEHGNVPLHYA 107
Cdd:PHA02878 272 alhssikSERKLKLLLEYGADINSLNSYKLTPLSSA 307
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 26-107 9.55e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 53.53  E-value: 9.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068458  26 DLNQGDDHGFSPLHWACREG-RSAVVEMLIMRGARINVMNRGDDTPLHLAAS-HGHRDIVQKLLQYKADINAVNEHGNVP 103
Cdd:PHA02876 299 DVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTP 378


                 ....
gi 149068458 104 LHYA 107
Cdd:PHA02876 379 IHYA 382
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
8-101 1.29e-08

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 52.65  E-value: 1.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068458   8 CREGNAVAVRLWLDNtENDLNQGDDHGFSPLHWACREGRSAVVEMLIMRGARINVMNRGDDTPLHLAASHGHRDIVQKLL 87
Cdd:COG0666  194 AENGHLEIVKLLLEA-GADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLL 272

                         90
                 ....*....|....
gi 149068458  88 QYKADINAVNEHGN 101
Cdd:COG0666  273 LALLLLAAALLDLL 286
PHA03095 PHA03095
ankyrin-like protein; Provisional
 26-104 1.78e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 52.72  E-value: 1.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068458  26 DLNQGDDHGFSPLHWACREG--RSAVVEMLIMRGARINVMNRGDDTPLHLAASHGHRDIVQKLLQYKADINAVNEHGNVP 103
Cdd:PHA03095 214 DPAATDMLGNTPLHSMATGSscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTP 293


                 .
gi 149068458 104 L 104
Cdd:PHA03095 294 L 294
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 22-107 2.62e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 51.97  E-value: 2.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068458  22 NTENDLNQGDDHGFSPLHWACREGRSA-VVEMLIMRGARINVMNRGDDTPLHLAASHGH-----RDIVQKLLQYKADINA 95
Cdd:PHA03100  22 IMEDDLNDYSYKKPVLPLYLAKEARNIdVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNA 101

                         90
                 ....*....|..
gi 149068458  96 VNEHGNVPLHYA 107
Cdd:PHA03100 102 PDNNGITPLLYA 113
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 27-107 3.29e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 51.99  E-value: 3.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068458  27 LNQGDDHGFSPLHWACRE-GRSAVVEMLIMRGARINVMNRGDDTPLHLAASHGH-RDIVQKLLQYKADINAVNEHGNVPL 104
Cdd:PHA02876 266 VNSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPL 345


                 ...
gi 149068458 105 HYA 107
Cdd:PHA02876 346 HQA 348
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 10-118 3.75e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 51.53  E-value: 3.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068458  10 EGNAVAVRLWLDNTE--NDLNQGDdhGFSPLHWACREGRSAVVEMLIMRGARINVMNRGDDTPLHLAASHGHRDIVQKLL 87
Cdd:PHA02875  78 EGDVKAVEELLDLGKfaDDVFYKD--GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLI 155

                         90       100       110
                 ....*....|....*....|....*....|.
gi 149068458  88 QYKADINAVNEHGNVPLHYACFWGQDQVAEV 118
Cdd:PHA02875 156 DHKACLDIEDCCGCTPLIIAMAKGDIAICKM 186
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 27-107 5.36e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 51.12  E-value: 5.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068458  27 LNQGDDHGFSPLHWACREGRSAVVEMLIMRGARINVMNRGDDTPLHLAASHgHRDIVQkLLQYKADINAVNEHGNVPLHY 106
Cdd:PHA02874 183 ANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIH-NRSAIE-LLINNASINDQDIDGSTPLHH 260


                 .
gi 149068458 107 A 107
Cdd:PHA02874 261 A 261
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 67-95 1.43e-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: 45.66  E-value: 1.43e-07
                           10        20
                   ....*....|....*....|....*....
gi 149068458    67 DDTPLHLAASHGHRDIVQKLLQYKADINA 95
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 26-120 1.50e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 50.06  E-value: 1.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068458  26 DLNQGDDHGFSPLHWACREGRSA-VVEMLIMRGARINVMNRGDDTPLHLAASHGHRDIVQKLLQYKADINAVNEHGNVPL 104
Cdd:PHA02876 333 DVNAADRLYITPLHQASTLDRNKdIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTAL 412

                         90
                 ....*....|....*.
gi 149068458 105 HYAcFWGQDQVAEVST 120
Cdd:PHA02876 413 HFA-LCGTNPYMSVKT 427
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 68-98 6.31e-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: 43.82  E-value: 6.31e-07
                          10        20        30
                  ....*....|....*....|....*....|..
gi 149068458   68 DTPLHLAASH-GHRDIVQKLLQYKADINAVNE 98
Cdd:pfam00023   3 NTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 9-107 9.16e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 47.65  E-value: 9.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068458   9 REGNAVAVRLWLdNTENDLNQGDDHGFSPLHWACREGRSAVVEMLIMRGA-----------------------RINVMNR 65
Cdd:PHA02874  44 RSGDAKIVELFI-KHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVdtsilpipciekdmiktildcgiDVNIKDA 122

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 149068458  66 GDDTPLHLAASHGHRDIVQKLLQYKADINAVNEHGNVPLHYA 107
Cdd:PHA02874 123 ELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIA 164
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 69-95 2.20e-06

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: 42.24  E-value: 2.20e-06
                          10        20
                  ....*....|....*....|....*..
gi 149068458   69 TPLHLAASHGHRDIVQKLLQYKADINA 95
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADINA 30
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 4-108 3.08e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 45.58  E-value: 3.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068458   4 IFTQCREGNAVAVRLW--LDNTENDLNQgddhgfSPLHwACREGRSAVVEM---LIMRGARINVMNRGDD-TPLHLAASH 77
Cdd:PHA02859  25 LFYYVEKDDIEGVKKWikFVNDCNDLYE------TPIF-SCLEKDKVNVEIlkfLIENGADVNFKTRDNNlSALHHYLSF 97

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 149068458  78 GHR---DIVQKLLQYKADINAVNEHGNVPLH-YAC 108
Cdd:PHA02859  98 NKNvepEILKILIDSGSSITEEDEDGKNLLHmYMC 132
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 18-119 3.15e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 46.01  E-value: 3.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068458  18 LWLDNTENDLNQGDDhgfSPLHWACREGRSAVVEMLIMRGARINVMNRGDDTPLHLAASHGHRDIVQKLLQYKADINAVN 97
Cdd:PLN03192 512 LLGDNGGEHDDPNMA---SNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRD 588

                         90       100
                 ....*....|....*....|....*....
gi 149068458  98 EHGNVPL-------HYACFWGQDQVAEVS 119
Cdd:PLN03192 589 ANGNTALwnaisakHHKIFRILYHFASIS 617
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 33-62 3.16e-06

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: 41.86  E-value: 3.16e-06
                          10        20        30
                  ....*....|....*....|....*....|
gi 149068458   33 HGFSPLHWACREGRSAVVEMLIMRGARINV 62
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 12-118 4.00e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 45.66  E-value: 4.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068458  12 NAVAVRLWLDNTENDLNQGDDHGFS-PLHWACREGRSAVVEMLIMRGARINVMNRGDDTPLHLAASHGHRDIVQKLLQYK 90
Cdd:PTZ00322  59 NKDATPDHNLTTEEVIDPVVAHMLTvELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFG 138

                         90       100
                 ....*....|....*....|....*...
gi 149068458  91 ADINAVNEHGNVPLHYACFWGQDQVAEV 118
Cdd:PTZ00322 139 ADPTLLDKDGKTPLELAEENGFREVVQL 166
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 38-104 4.67e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.82  E-value: 4.67e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 149068458  38 LHWA-CREGRSAVVEMLIMRGARINVMNRGDDTPLHLAASHGHR-DIVQKLLQYKADINAVNEHGNVPL 104
Cdd:PHA02876 412 LHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAINIQNQYPL 480
PHA02946 PHA02946
ankyin-like protein; Provisional
 28-108 5.39e-06

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 45.43  E-value: 5.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068458  28 NQGDDHGFSPLHWACREGRSAVVEMLIMRGARINVMNRGDDTPLHLAASHGHRDI--VQKLLQYKADI-NAVNEHGNVPL 104
Cdd:PHA02946  66 NETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIerINLLVQYGAKInNSVDEEGCGPL 145


                 ....
gi 149068458 105 hYAC 108
Cdd:PHA02946 146 -LAC 148
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 5-93 8.15e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.05  E-value: 8.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068458   5 FTQCREGNAVAVRLWLDNTENdLNQGDDHGFSPLHWACREG-RSAVVEMLIMRGARINVMNRGDDTPLHLAAshGHRDIV 83
Cdd:PHA02876 414 FALCGTNPYMSVKTLIDRGAN-VNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIV 490

                         90
                 ....*....|
gi 149068458  84 QKLLQYKADI 93
Cdd:PHA02876 491 NILLHYGAEL 500
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 49-107 1.53e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 44.28  E-value: 1.53e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 149068458  49 VVEMLIMRGARINVMNRGDDTPLHLAASHGHRDIVQKLLQYKADINAVNEHGNVPLHYA 107
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECA 218
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 33-62 1.59e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.88  E-value: 1.59e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 149068458    33 HGFSPLHWACREGRSAVVEMLIMRGARINV 62
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA03095 PHA03095
ankyrin-like protein; Provisional
 26-121 2.12e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 43.47  E-value: 2.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068458  26 DLNQGDDHGFSPLHWACREGRSAVVEMLIMRGARINVMNRGDDTPLHLAASHGHRDIVQKLLQYKADINAVNEhgnvPLH 105
Cdd:PHA03095 249 SINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAA----TLN 324

                         90
                 ....*....|....*.
gi 149068458 106 YACFWGQDQVAEVSTQ 121
Cdd:PHA03095 325 TASVAGGDIPSDATRL 340
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 33-65 3.73e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.19  E-value: 3.73e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 149068458   33 HGFSPLHWAC-REGRSAVVEMLIMRGARINVMNR 65
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 34-105 4.28e-05

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 42.69  E-value: 4.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068458  34 GFSPLHWACREGRSAVVEMLIMRGARIN---------VMNRGD-----DTPLHLAASHGHRDIVQKLLQYKADINAVNEH 99
Cdd:cd22192   89 GETALHIAVVNQNLNLVRELIARGADVVspratgtffRPGPKNliyygEHPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168


                 ....*.
gi 149068458 100 GNVPLH 105
Cdd:cd22192  169 GNTVLH 174
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 26-107 4.83e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 42.74  E-value: 4.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068458  26 DLNQGDDHGFSPLHWACREGRSAVVEMLIMRGARINVMNRGDDTPLHLAASHGHRDIVQKLLQYKADI------------ 93
Cdd:PHA02876 170 DVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNInkndlsllkair 249

                         90       100       110
                 ....*....|....*....|....*....|.
gi 149068458  94 -----------------NAVNEHGNVPLHYA 107
Cdd:PHA02876 250 nedletslllydagfsvNSIDDCKNTPLHHA 280
PHA02946 PHA02946
ankyin-like protein; Provisional
 50-106 5.13e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 42.35  E-value: 5.13e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 149068458  50 VEMLIMRGARINVMNRGDDTPLHLAASHGHRDIVQKLLQYKADINAVNEHGNVPLHY 106
Cdd:PHA02946  55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYY 111
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 31-124 6.40e-05

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 41.02  E-value: 6.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068458  31 DDHGFSPLHWACREGrsAVVEMLIMRGARINV-------MNRGDDTPLHLAASHGHRDIVQK---LLQYKADINAVNE-H 99
Cdd:PHA02736  14 DIEGENILHYLCRNG--GVTDLLAFKNAISDEnrylvleYNRHGKQCVHIVSNPDKADPQEKlklLMEWGADINGKERvF 91

                         90       100
                 ....*....|....*....|....*
gi 149068458 100 GNVPLHYACFWGQDQVAEVSTQTPG 124
Cdd:PHA02736  92 GNTPLHIAVYTQNYELATWLCNQPG 116
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 34-105 1.16e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 41.33  E-value: 1.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068458  34 GFSPLHWACREGRSAVVEMLIMRGARINVMNRGD--------------DTPLHLAASHGHRDIVQKLLQ---YKADINAV 96
Cdd:cd22196   94 GQTALHIAIERRNMHLVELLVQNGADVHARASGEffkkkkggpgfyfgELPLSLAACTNQLDIVKFLLEnphSPADISAR 173


                 ....*....
gi 149068458  97 NEHGNVPLH 105
Cdd:cd22196  174 DSMGNTVLH 182
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 34-105 1.94e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 40.93  E-value: 1.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068458  34 GFSPLHWACREGRSAVVEMLIMRGARINVMNRGD--------------DTPLHLAASHGHRDIVQKLLQ---YKADINAV 96
Cdd:cd22193   76 GQTALHIAIERRQGDIVALLVENGADVHAHAKGRffqpkyqgegfyfgELPLSLAACTNQPDIVQYLLEnehQPADIEAQ 155


                 ....*....
gi 149068458  97 NEHGNVPLH 105
Cdd:cd22193  156 DSRGNTVLH 164
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 33-105 2.08e-04

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: 40.83  E-value: 2.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068458   33 HGFSPLHWACREGRSAVVEMLIMRGARINVMNRGDD--------------TPLHLAASHGHRDIVQKLLQYKADINAVNE 98
Cdd:TIGR00870 127 PGITALHLAAHRQNYEIVKLLLERGASVPARACGDFfvksqgvdsfyhgeSPLNAAACLGSPSIVALLSEDPADILTADS 206


                  ....*..
gi 149068458   99 HGNVPLH 105
Cdd:TIGR00870 207 LGNTLLH 213
PHA02791 PHA02791
ankyrin-like protein; Provisional
 23-118 2.28e-04

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 40.41  E-value: 2.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068458  23 TENDLNQGDDHGFSPLHWACREGRSAVVEMLIMRGARINVMNrgDDTPLHLAASHGHRDIVQKLLQYKADINAVNEHGNV 102
Cdd:PHA02791  19 SSKDAFKADVHGHSALYYAIADNNVRLVCTLLNAGALKNLLE--NEFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNT 96

                         90
                 ....*....|....*.
gi 149068458 103 PLHYACFWGQDQVAEV 118
Cdd:PHA02791  97 ALYYAVDSGNMQTVKL 112
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 27-96 2.88e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 40.36  E-value: 2.88e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 149068458  27 LNQGDDHGFSPLHWACREGRSAVVEMLIMRGARIN-VMNRGDDTPLHLAASHGHRDIVQKLLQYKADINAV 96
Cdd:PHA02875 161 LDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDyFGKNGCVAALCYAIENNKIDIVRLFIKRGADCNIM 231
PHA03095 PHA03095
ankyrin-like protein; Provisional
 49-109 3.56e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 40.01  E-value: 3.56e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 149068458  49 VVEMLIMRGARINVMNRGDDTPLHL---AASHGHRDIVQKLLQYKADINAVNEHGNVPLH-YACF 109
Cdd:PHA03095  29 EVRRLLAAGADVNFRGEYGKTPLHLylhYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHlYLYN 93
PHA02798 PHA02798
ankyrin-like protein; Provisional
 26-96 4.31e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 39.82  E-value: 4.31e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 149068458  26 DLNQGDDHGFSPLHWACREGRSAVVEMLIMRGARINVMNRGDDTPLHLAASHGHRDIVQKLLQYKADINAV 96
Cdd:PHA02798 250 DINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNKKPNKNTI 320
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 34-107 5.34e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 39.59  E-value: 5.34e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 149068458  34 GFSPLHWACREGRSAVVEMLIMRGARINVMNRGDDTPLHLAASHGHRDIVQKLLQYKADINAV-NEHGNVPLHYA 107
Cdd:PHA02875  35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVfYKDGMTPLHLA 109
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 35-104 1.44e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 38.05  E-value: 1.44e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068458  35 FSPLHWACREGRSAVVEMLIMRGARINVMNRGDDTPLHLAASHGHRDIVQKLLQYKADINAVNEHGNVPL 104
Cdd:PHA02875 136 FSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAA 205
Ank_4 pfam13637
Ankyrin repeats (many copies);
4-54 3.02e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 34.56  E-value: 3.02e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 149068458    4 IFTQCREGNAVAVRLWLDNTeNDLNQGDDHGFSPLHWACREGRSAVVEMLI 54
Cdd:pfam13637   5 LHAAAASGHLELLRLLLEKG-ADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02743 PHA02743
Viral ankyrin protein; Provisional
 8-109 3.34e-03

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 36.33  E-value: 3.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068458   8 CREGNA---VAVRLWLDNTENDLNQGDDHGFSPLHWACREGRSAVV---EMLIMRGARINVMNRG-DDTPLHLAASHGHR 80
Cdd:PHA02743  28 CRTGNIyelMEVAPFISGDGHLLHRYDHHGRQCTHMVAWYDRANAVmkiELLVNMGADINARELGtGNTLLHIAASTKNY 107

                         90       100       110
                 ....*....|....*....|....*....|
gi 149068458  81 DIVQKLL-QYKADINAVNEHGNVPLHYACF 109
Cdd:PHA02743 108 ELAEWLCrQLGVNLGAINYQHETAYHIAYK 137
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 20-107 4.07e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 36.78  E-value: 4.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068458  20 LDNTENDLNQGDDHGFSPLHWACREGRSAVVEMLIMRGARINVMNRGDDTPLHLAASH---------------------- 77
Cdd:PHA02878  23 IDHTENYSTSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEpnklgmkemirsinkcsvfytl 102

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 149068458  78 ------------------------GHRD------------------IVQKLLQYKADINAVNEH-GNVPLHYA 107
Cdd:PHA02878 103 vaikdafnnrnveifkiiltnrykNIQTidlvyidkkskddiieaeITKLLLSYGADINMKDRHkGNTALHYA 175
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 62-110 6.48e-03

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: 36.21  E-value: 6.48e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 149068458   62 VMNRGDDTPLHLAASHGHRDIVQKLLQYKADINAVNEHGNVPLHYACFW 110
Cdd:TIGR00870 252 ILNHQGLTPLKLAAKEGRIVLFRLKLAIKYKQKKFVAWPNGQQLLSLYW 300
 
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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