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Conserved domains on  [gi|2416958208|ref|XP_052674099|]
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histone-lysine N-methyltransferase EHMT1-like [Crassostrea angulata]

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];
15-192 1.36e-31

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 116.59  E-value: 1.36e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416958208  15 VNNGDYSTVKKQLKLGADPNIYDEEGNPLLFLPIINGDDEMMDILLSFdKCNINIISYDLRTPLLIAVELDDLEFVKSLI 94
Cdd:COG0666    95 ARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA-GADVNAQDNDGNTPLHLAAANGNLEIVKLLL 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416958208  95 KSGANIDCIDGSGKTPLLLALEEGRFEIAEYLMKRGCNVNAVDGLGQSALHFVANGTHSHCIKMVDKIMKNGFKLEENNE 174
Cdd:COG0666   174 EAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGL 253

                         170
                  ....*....|....*...
gi 2416958208 175 WIPAASVKSRTIGRKTKL 192
Cdd:COG0666   254 TALLLAAAAGAALIVKLL 271
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
15-192 1.36e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 116.59  E-value: 1.36e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416958208  15 VNNGDYSTVKKQLKLGADPNIYDEEGNPLLFLPIINGDDEMMDILLSFdKCNINIISYDLRTPLLIAVELDDLEFVKSLI 94
Cdd:COG0666    95 ARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA-GADVNAQDNDGNTPLHLAAANGNLEIVKLLL 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416958208  95 KSGANIDCIDGSGKTPLLLALEEGRFEIAEYLMKRGCNVNAVDGLGQSALHFVANGTHSHCIKMVDKIMKNGFKLEENNE 174
Cdd:COG0666   174 EAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGL 253

                         170
                  ....*....|....*...
gi 2416958208 175 WIPAASVKSRTIGRKTKL 192
Cdd:COG0666   254 TALLLAAAAGAALIVKLL 271
Ank_2 pfam12796
Ankyrin repeats (3 copies);
14-104 1.66e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 66.29  E-value: 1.66e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416958208  14 CVNNGDYSTVKKQLKLGADPNIYDEEGNPLLFLPIINGDDEMMDILLsfDKCNINIISYDlRTPLLIAVELDDLEFVKSL 93
Cdd:pfam12796   4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL--EHADVNLKDNG-RTALHYAARSGHLEIVKLL 80

                          90
                  ....*....|.
gi 2416958208  94 IKSGANIDCID 104
Cdd:pfam12796  81 LEKGADINVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 1-166 3.34e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.93  E-value: 3.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416958208   1 MEVNTISD-------KEFVKCVNNGDYSTVKKQLKLG--ADPNIYdEEGNPLLFLPIINGDDEMMDILLSFdKCNINIIS 71
Cdd:PHA02875   55 MKHGAIPDvkypdieSELHDAVEEGDVKAVEELLDLGkfADDVFY-KDGMTPLHLATILKKLDIMKLLIAR-GADPDIPN 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416958208  72 YDLRTPLLIAVELDDLEFVKSLIKSGANIDCIDGSGKTPLLLALEEGRFEIAEYLMKRGCNVNAVDGLGQSALhfVANGT 151
Cdd:PHA02875  133 TDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAA--LCYAI 210

                         170
                  ....*....|....*
gi 2416958208 152 HSHCIKMVDKIMKNG 166
Cdd:PHA02875  211 ENNKIDIVRLFIKRG 225
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 46-174 9.52e-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: 48.60  E-value: 9.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416958208  46 LPIINGDDEMMDILLSFDKCN------INII----SYDLRTPLLIAVELDDLEFVKSLIKSGANID-CIDGS-------- 106
Cdd:cd22194   103 LNINENTKEIVRILLAFAEENgildrfINAEyteeAYEGQTALNIAIERRQGDIVKLLIAKGADVNaHAKGVffnpkykh 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416958208 107 -----GKTPLLLALEEGRFEIAEYLMKRG-CNVNAVDGLGQSALH---FVANGTHSH---CIKMVDKIMK--NGFKLEE- 171
Cdd:cd22194   183 egfyfGETPLALAACTNQPEIVQLLMEKEsTDITSQDSRGNTVLHalvTVAEDSKTQndfVKRMYDMILLksENKNLETi 262


                  ....
gi 2416958208 172 -NNE 174
Cdd:cd22194   263 rNNE 266
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 76-145 2.06e-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: 41.61  E-value: 2.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416958208  76 TPLLIAVELDDLEFVKSLIKSGANI-------DCIDGSGKT-------PLLLALEEGRFEIAEYLMKRGCNVNAVDGLGQ 141
Cdd:TIGR00870 130 TALHLAAHRQNYEIVKLLLERGASVparacgdFFVKSQGVDsfyhgesPLNAAACLGSPSIVALLSEDPADILTADSLGN 209


                  ....
gi 2416958208 142 SALH 145
Cdd:TIGR00870 210 TLLH 213
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 107-135 1.73e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.87  E-value: 1.73e-03
                           10        20
                   ....*....|....*....|....*....
gi 2416958208  107 GKTPLLLALEEGRFEIAEYLMKRGCNVNA 135
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
15-192 1.36e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 116.59  E-value: 1.36e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416958208  15 VNNGDYSTVKKQLKLGADPNIYDEEGNPLLFLPIINGDDEMMDILLSFdKCNINIISYDLRTPLLIAVELDDLEFVKSLI 94
Cdd:COG0666    95 ARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA-GADVNAQDNDGNTPLHLAAANGNLEIVKLLL 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416958208  95 KSGANIDCIDGSGKTPLLLALEEGRFEIAEYLMKRGCNVNAVDGLGQSALHFVANGTHSHCIKMVDKIMKNGFKLEENNE 174
Cdd:COG0666   174 EAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGL 253

                         170
                  ....*....|....*...
gi 2416958208 175 WIPAASVKSRTIGRKTKL 192
Cdd:COG0666   254 TALLLAAAAGAALIVKLL 271
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
15-166 4.16e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 107.35  E-value: 4.16e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416958208  15 VNNGDYSTVKKQLKLGADPNIYDEEGNPLLFLPIINGDDEMMDILLSfDKCNINIISYDLRTPLLIAVELDDLEFVKSLI 94
Cdd:COG0666    62 ALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLE-AGADVNARDKDGETPLHLAAYNGNLEIVKLLL 140

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2416958208  95 KSGANIDCIDGSGKTPLLLALEEGRFEIAEYLMKRGCNVNAVDGLGQSALHFVAngtHSHCIKMVDKIMKNG 166
Cdd:COG0666   141 EAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAA---ENGHLEIVKLLLEAG 209
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
15-174 1.16e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 98.49  E-value: 1.16e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416958208  15 VNNGDYSTVKKQLKLGADPNIYDEEGNPLLFLPIINGDDEMMDILLSFdKCNINIISYDLRTPLLIAVELDDLEFVKSLI 94
Cdd:COG0666   128 AYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA-GADVNARDNDGETPLHLAAENGHLEIVKLLL 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416958208  95 KSGANIDCIDGSGKTPLLLALEEGRFEIAEYLMKRGCNVNAVDGLGQSALHFVANGTHSHCIKMVDKIMKNGFKLEENNE 174
Cdd:COG0666   207 EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLL 286
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
23-166 5.27e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 91.17  E-value: 5.27e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416958208  23 VKKQLKLGADPNIYDEEGNPLLFLPIINGDDEMMDILLSFDKCNINIISYDLRTPLLIAVELDDLEFVKSLIKSGANIDC 102
Cdd:COG0666    36 LLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNA 115

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2416958208 103 IDGSGKTPLLLALEEGRFEIAEYLMKRGCNVNAVDGLGQSALHFVAngtHSHCIKMVDKIMKNG 166
Cdd:COG0666   116 RDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA---ANGNLEIVKLLLEAG 176
Ank_2 pfam12796
Ankyrin repeats (3 copies);
14-104 1.66e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 66.29  E-value: 1.66e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416958208  14 CVNNGDYSTVKKQLKLGADPNIYDEEGNPLLFLPIINGDDEMMDILLsfDKCNINIISYDlRTPLLIAVELDDLEFVKSL 93
Cdd:pfam12796   4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL--EHADVNLKDNG-RTALHYAARSGHLEIVKLL 80

                          90
                  ....*....|.
gi 2416958208  94 IKSGANIDCID 104
Cdd:pfam12796  81 LEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
78-173 1.50e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.98  E-value: 1.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416958208  78 LLIAVELDDLEFVKSLIKSGANIDCIDGSGKTPLLLALEEGRFEIAEYLMKRgCNVNAVDGlGQSALHFVAngtHSHCIK 157
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAA---RSGHLE 75

                          90
                  ....*....|....*.
gi 2416958208 158 MVDKIMKNGFKLEENN 173
Cdd:pfam12796  76 IVKLLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
17-144 1.62e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 64.98  E-value: 1.62e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416958208  17 NGDYSTVKKQLKLGADPNIYDEEGNPLLFLPIINGDDEMMDILLSFdKCNINIISYDLRTPLLIAVELDDLEFVKSLIKS 96
Cdd:COG0666   163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA-GADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2416958208  97 GANIDCIDGSGKTPLLLALEEGRFEIAEYLMKRGCNVNAVDGLGQSAL 144
Cdd:COG0666   242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
27-166 8.26e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 63.05  E-value: 8.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416958208  27 LKLGADPNIYDEEGNPLLFLPIINGDDEMMDILLSFDKCNINIISYDLRTPLLIAVELDDLEFVKSLIKSGANIDCIDGS 106
Cdd:COG0666     7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416958208 107 GKTPLLLALEEGRFEIAEYLMKRGCNVNAVDGLGQSALHFVANGTHshcIKMVDKIMKNG 166
Cdd:COG0666    87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGN---LEIVKLLLEAG 143
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 1-166 3.34e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.93  E-value: 3.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416958208   1 MEVNTISD-------KEFVKCVNNGDYSTVKKQLKLG--ADPNIYdEEGNPLLFLPIINGDDEMMDILLSFdKCNINIIS 71
Cdd:PHA02875   55 MKHGAIPDvkypdieSELHDAVEEGDVKAVEELLDLGkfADDVFY-KDGMTPLHLATILKKLDIMKLLIAR-GADPDIPN 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416958208  72 YDLRTPLLIAVELDDLEFVKSLIKSGANIDCIDGSGKTPLLLALEEGRFEIAEYLMKRGCNVNAVDGLGQSALhfVANGT 151
Cdd:PHA02875  133 TDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAA--LCYAI 210

                         170
                  ....*....|....*
gi 2416958208 152 HSHCIKMVDKIMKNG 166
Cdd:PHA02875  211 ENNKIDIVRLFIKRG 225
Ank_4 pfam13637
Ankyrin repeats (many copies);
75-126 5.17e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.43  E-value: 5.17e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2416958208  75 RTPLLIAVELDDLEFVKSLIKSGANIDCIDGSGKTPLLLALEEGRFEIAEYL 126
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 22-174 6.43e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 58.14  E-value: 6.43e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416958208  22 TVKKQLKLGADPNIYDEEGNPLLFLPIIN--GDDEMMDILLSFdKCNINIISYDLRTPLLIAVE--LDDLEFVKSLIKSG 97
Cdd:PHA03100   88 IVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDN-GANVNIKNSDGENLLHLYLEsnKIDLKILKLLIDKG 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416958208  98 ANIDCI----------------DGSGKTPLLLALEEGRFEIAEYLMKRGCNVNAVDGLGQSALHFVANGTHSHCIKMV-- 159
Cdd:PHA03100  167 VDINAKnrvnyllsygvpinikDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLln 246

                         170
                  ....*....|....*....
gi 2416958208 160 ----DKIMKNGFKLEENNE 174
Cdd:PHA03100  247 ngpsIKTIIETLLYFKDKD 265
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 23-136 2.05e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 56.54  E-value: 2.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416958208  23 VKKQLKLGADPNIYDEEGNPLLFLPIINGDDEMMDILLSFDKCnINIISYDLRTPLLIAVELDDLEFVKSLIKSGANIDC 102
Cdd:PHA02875  118 MKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKAC-LDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDY 196

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2416958208 103 IDGSGKTPLL-LALEEGRFEIAEYLMKRGCNVNAV 136
Cdd:PHA02875  197 FGKNGCVAALcYAIENNKIDIVRLFIKRGADCNIM 231
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 46-159 3.58e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 55.74  E-value: 3.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416958208  46 LPIINGDDEMMDILLSfDKCNINIISYDLRTPLLIAVELDDLEFVKSLIKSGANIDCIDGSGKTPLLLALEEGRFEIAEY 125
Cdd:PHA02874   97 LPIPCIEKDMIKTILD-CGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKL 175

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2416958208 126 LMKRGCNVNAVDGLGQSALHFVANGTHSHCIKMV 159
Cdd:PHA02874  176 LLEKGAYANVKDNNGESPLHNAAEYGDYACIKLL 209
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 27-137 6.99e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 55.26  E-value: 6.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416958208  27 LKLGADPNIYDEEGNPLLFLPIINGDDEMMDILLSFDKCNINIISYDLrtpLLIAVELDDLEFVKSLIKSGANIDCIDGS 106
Cdd:PLN03192  578 LKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAGDL---LCTAAKRNDLTAMKELLKQGLNVDSEDHQ 654

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2416958208 107 GKTPLLLALEEGRFEIAEYLMKRGCNVNAVD 137
Cdd:PLN03192  655 GATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 12-145 7.86e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 54.97  E-value: 7.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416958208  12 VKCVNNgdySTVKKQLKLGADPNIYDEEGNPLLFLPIINGDDEMMDILLSFdKCNINIISYDLRTPLLIAVELDDLEFVK 91
Cdd:PHA02874   99 IPCIEK---DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEY-GADVNIEDDNGCYPIHIAIKHNFFDIIK 174

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2416958208  92 SLIKSGANIDCIDGSGKTPLLLALEEGRFEIAEYLMKRGCNVNAVDGLGQSALH 145
Cdd:PHA02874  175 LLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLH 228
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 15-149 2.83e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.04  E-value: 2.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416958208  15 VNNGDYSTVKKQLKLGADPNIYDEEGNPLLFLPIINGDDEMMDILLSfDKCNINIISYDLRTPLLIAVELDDLEFVKSLI 94
Cdd:PHA02874  132 IKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLE-KGAYANVKDNNGESPLHNAAEYGDYACIKLLI 210

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2416958208  95 KSGANIDCIDGSGKTPLLLALEEGRFEIAEYLMKRGCNVNAVDglGQSALHFVAN 149
Cdd:PHA02874  211 DHGNHIMNKCKNGFTPLHNAIIHNRSAIELLINNASINDQDID--GSTPLHHAIN 263
Ank_4 pfam13637
Ankyrin repeats (many copies);
109-158 9.97e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.27  E-value: 9.97e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2416958208 109 TPLLLALEEGRFEIAEYLMKRGCNVNAVDGLGQSALHFVANGTHSHCIKM 158
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKL 52
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 65-174 1.02e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 51.59  E-value: 1.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416958208  65 CNINIISYDLRTPL-----LIAVELDDLEFVKSLIKSGANIDCIDGSGKTPLLLALEE--GRFEIAEYLMKRGCNVNAVD 137
Cdd:PHA03100   59 ADINSSTKNNSTPLhylsnIKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKN 138

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2416958208 138 GLGQSALHFVANGTHSHcIKMVDKIMKNGFKLEENNE 174
Cdd:PHA03100  139 SDGENLLHLYLESNKID-LKILKLLIDKGVDINAKNR 174
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 50-128 2.29e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.67  E-value: 2.29e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2416958208  50 NGDDEMMDILLSfDKCNINIISYDLRTPLLIAVELDDLEFVKSLIKSGANIDCIDGSGKTPLLLALEEGRFEIAEYLMK 128
Cdd:PTZ00322   92 SGDAVGARILLT-GGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 46-174 9.52e-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: 48.60  E-value: 9.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416958208  46 LPIINGDDEMMDILLSFDKCN------INII----SYDLRTPLLIAVELDDLEFVKSLIKSGANID-CIDGS-------- 106
Cdd:cd22194   103 LNINENTKEIVRILLAFAEENgildrfINAEyteeAYEGQTALNIAIERRQGDIVKLLIAKGADVNaHAKGVffnpkykh 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416958208 107 -----GKTPLLLALEEGRFEIAEYLMKRG-CNVNAVDGLGQSALH---FVANGTHSH---CIKMVDKIMK--NGFKLEE- 171
Cdd:cd22194   183 egfyfGETPLALAACTNQPEIVQLLMEKEsTDITSQDSRGNTVLHalvTVAEDSKTQndfVKRMYDMILLksENKNLETi 262


                  ....
gi 2416958208 172 -NNE 174
Cdd:cd22194   263 rNNE 266
PHA03095 PHA03095
ankyrin-like protein; Provisional
 85-145 4.91e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.56  E-value: 4.91e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2416958208  85 DDLEFVKSLIKSGANIDCIDGSGKTPLLLALEEG-RFEIAEYLMKRGCNVNAVDGLGQSALH 145
Cdd:PHA03095   61 KVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNAtTLDVIKLLIKAGADVNAKDKVGRTPLH 122
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 78-153 2.55e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 44.47  E-value: 2.55e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2416958208  78 LLIAVELDDLEFVKSLIKSGANIDCIDGSGKTPLLLALEEGRFEIAEYLMKRGCNVNAVDGLGQSAL-HFVANGTHS 153
Cdd:PLN03192  529 LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwNAISAKHHK 605
Ank_5 pfam13857
Ankyrin repeats (many copies);
59-114 2.65e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.41  E-value: 2.65e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2416958208  59 LLSFDKCNINIISYDLRTPLLIAVELDDLEFVKSLIKSGANIDCIDGSGKTPLLLA 114
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 23-154 3.37e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 44.28  E-value: 3.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416958208  23 VKKQLKLGADPNIYDEEGNPLLFLPIING-DDEMMDILLSFDkCNINIISYDLRTPLLIAVELD-DLEFVKSLIKSGANI 100
Cdd:PHA02876  290 VPKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLG-ADVNAADRLYITPLHQASTLDrNKDIVITLLELGANV 368

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2416958208 101 DCIDGSGKTPLLLALEEGRFEIAEYLMKRGCNVNAVDGLGQSALHFVANGTHSH 154
Cdd:PHA02876  369 NARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPY 422
Ank_5 pfam13857
Ankyrin repeats (many copies);
98-147 8.81e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.25  E-value: 8.81e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2416958208  98 ANIDCIDGSGKTPLLLALEEGRFEIAEYLMKRGCNVNAVDGLGQSALHFV 147
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 72-172 1.60e-04

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: 42.15  E-value: 1.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416958208  72 YDLRTPLLIAVELDDLEFVKSLIKSGANIDCIDGS-------------GKTPLLLALEEGRFEIAEYLMKRG---CNVNA 135
Cdd:cd22197    92 YRGHSALHIAIEKRSLQCVKLLVENGADVHARACGrffqkkqgtcfyfGELPLSLAACTKQWDVVNYLLENPhqpASLQA 171

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2416958208 136 VDGLGQSALH---FVANGTHSH---CIKMVDKIMKNGFKLEEN 172
Cdd:cd22197   172 QDSLGNTVLHalvMIADNSPENsalVIKMYDGLLQAGARLCPT 214
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 72-163 1.91e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 41.92  E-value: 1.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416958208  72 YDLRTPLLIAVELDDLEFVKSLIKSGA--------------NIDCIDGSGKTPLLLALEEGRFEIAEYLMKRGCNVNAVD 137
Cdd:cd22192    87 YQGETALHIAVVNQNLNLVRELIARGAdvvspratgtffrpGPKNLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQD 166

                          90       100
                  ....*....|....*....|....*...
gi 2416958208 138 GLGQSALHFVA--NGTHSHCiKMVDKIM 163
Cdd:cd22192   167 SLGNTVLHILVlqPNKTFAC-QMYDLIL 193
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 76-145 2.06e-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: 41.61  E-value: 2.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416958208  76 TPLLIAVELDDLEFVKSLIKSGANI-------DCIDGSGKT-------PLLLALEEGRFEIAEYLMKRGCNVNAVDGLGQ 141
Cdd:TIGR00870 130 TALHLAAHRQNYEIVKLLLERGASVparacgdFFVKSQGVDsfyhgesPLNAAACLGSPSIVALLSEDPADILTADSLGN 209


                  ....
gi 2416958208 142 SALH 145
Cdd:TIGR00870 210 TLLH 213
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 107-137 2.86e-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: 37.27  E-value: 2.86e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2416958208 107 GKTPLLLA-LEEGRFEIAEYLMKRGCNVNAVD 137
Cdd:pfam00023   2 GNTPLHLAaGRRGNLEIVKLLLSKGADVNARD 33
PHA03095 PHA03095
ankyrin-like protein; Provisional
 17-165 4.16e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 40.78  E-value: 4.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416958208  17 NGDYSTVKKQLKLGADPNIYDEEG-NPLlflpiingddemmDILLSFDKCNINIisydlrtplliavelddlefVKSLIK 95
Cdd:PHA03095  129 NINPKVIRLLLRKGADVNALDLYGmTPL-------------AVLLKSRNANVEL--------------------LRLLID 175

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2416958208  96 SGANIDCIDGSGKTPLLLALE--EGRFEIAEYLMKRGCNVNAVDGLGQSALHFVANGTHSHCIKMVDKIMKN 165
Cdd:PHA03095  176 AGADVYAVDDRFRSLLHHHLQsfKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVLPLLIAG 247
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 107-135 6.57e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.08  E-value: 6.57e-04
                          10        20
                  ....*....|....*....|....*....
gi 2416958208 107 GKTPLLLALEEGRFEIAEYLMKRGCNVNA 135
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02798 PHA02798
ankyrin-like protein; Provisional
 1-175 9.00e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 39.82  E-value: 9.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416958208   1 MEVNTISDkeFVKCVNNGDYSTVKKQLKLgADPNIYDEEGNplLFLPIINGDDEMMDILLSFDK--CNINIISYDLRTPL 78
Cdd:PHA02798    1 MDIDNLYN--YITFSDNVKLSTVKLLIKS-CNPNEIVNEYS--IFQKYLQRDSPSTDIVKLFINlgANVNGLDNEYSTPL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416958208  79 -LIAVELDD----LEFVKSLIKSGANIDCIDGSGKTPLLLALEEG---RFEIAEYLMKRGCNVNAVDGLGQSALHFVANG 150
Cdd:PHA02798   76 cTILSNIKDykhmLDIVKILIENGADINKKNSDGETPLYCLLSNGyinNLEILLFMIENGADTTLLDKDGFTMLQVYLQS 155

                         170       180
                  ....*....|....*....|....*
gi 2416958208 151 THSHCIKMVDKIMKNGFKLEENNEW 175
Cdd:PHA02798  156 NHHIDIEIIKLLLEKGVDINTHNNK 180
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 79-144 1.05e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 39.50  E-value: 1.05e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2416958208  79 LIAVELDDLEF------VKSLIKSGANIDCIDGSGKTPLLLALEEGRFEIAEYLMKRGCNVNAVDGLGQSAL 144
Cdd:PTZ00322   81 MLTVELCQLAAsgdavgARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPL 152
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 52-146 1.12e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 39.48  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416958208  52 DDEMMDILLSFDkCNINIISYD-LRTPLLIAVELDDLEFVKSLIKSGANIDCIDGSGKTPLLLALEEGRFEIAEYLMKRG 130
Cdd:PHA02878  146 EAEITKLLLSYG-ADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENG 224

                          90
                  ....*....|....*.
gi 2416958208 131 CNVNAVDGLGQSALHF 146
Cdd:PHA02878  225 ASTDARDKCGNTPLHI 240
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 107-135 1.73e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.87  E-value: 1.73e-03
                           10        20
                   ....*....|....*....|....*....
gi 2416958208  107 GKTPLLLALEEGRFEIAEYLMKRGCNVNA 135
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 18-157 1.83e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 38.89  E-value: 1.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416958208  18 GDYSTVKKQLKLGADPNIYDEEGNPLLFLPIingDDEMMDILLSFDKCNINIISYDLRtpLLIAVELDDLEFVKSLIKSG 97
Cdd:PHA02876  189 GNAKMVNLLLSYGADVNIIALDDLSVLECAV---DSKNIDTIKAIIDNRSNINKNDLS--LLKAIRNEDLETSLLLYDAG 263

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2416958208  98 ANIDCIDGSGKTPLLLALEEGRF-EIAEYLMKRGCNVNAVDGLGQSALHFVA-NGTHSHCIK 157
Cdd:PHA02876  264 FSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAkNGYDTENIR 325
PHA03095 PHA03095
ankyrin-like protein; Provisional
 19-115 2.85e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 38.08  E-value: 2.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416958208  19 DYSTVKKQLKLGADPNIYDEEGNPLLFLPIINGDDEMMDIL-LSFDKCNINIISYDLRTPLLIAVELDDLEFVKSLIKSG 97
Cdd:PHA03095  201 RARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVLpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALG 280

                          90
                  ....*....|....*...
gi 2416958208  98 ANIDCIDGSGKTPLLLAL 115
Cdd:PHA03095  281 ADINAVSSDGNTPLSLMV 298
PHA03095 PHA03095
ankyrin-like protein; Provisional
 86-166 3.21e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 38.08  E-value: 3.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416958208  86 DLEFVKSLIKSGANIDCIDGSGKTPLLLAL---EEGRFEIAEYLMKRGCNVNAVDGLGQSALHFVAngTHSHCIKMVDKI 162
Cdd:PHA03095   26 TVEEVRRLLAAGADVNFRGEYGKTPLHLYLhysSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYL--YNATTLDVIKLL 103


                  ....
gi 2416958208 163 MKNG 166
Cdd:PHA03095  104 IKAG 107
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 48-130 3.31e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 38.02  E-value: 3.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416958208  48 IINGDDEMMDILLSFDKCNINIISYDLRTPLLIAVELDDLEFVKSLIKSGANIDCIDGSGKTPLLLALEEGRFEIAEYLM 127
Cdd:PHA02874    9 IYSGDIEAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI 88


                  ...
gi 2416958208 128 KRG 130
Cdd:PHA02874   89 DNG 91
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 15-145 4.32e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 37.11  E-value: 4.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416958208  15 VNNGDYSTVKKQLKLGADPNIYDEegNPLLF-LPIINGDDEMMDILLSfDKCNIN-IISYDLRTPL---LIAVELDDLEF 89
Cdd:PHA02859   29 VEKDDIEGVKKWIKFVNDCNDLYE--TPIFScLEKDKVNVEILKFLIE-NGADVNfKTRDNNLSALhhyLSFNKNVEPEI 105

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2416958208  90 VKSLIKSGANIDCIDGSGKTPLLLALEEG--RFEIAEYLMKRGCNVNAVDGLGQSALH 145
Cdd:PHA02859  106 LKILIDSGSSITEEDEDGKNLLHMYMCNFnvRINVIKLLIDSGVSFLNKDFDNNNILY 163
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 64-169 5.21e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 37.34  E-value: 5.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416958208  64 KCNINIISYDLRTPLLIAVELDDLEFVKSLIKSGANIDCIDGSGKTPLLLALEEGR-----FEIAEYLMKRGCNVNAVDG 138
Cdd:PHA03100   25 DDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDN 104

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2416958208 139 LGQSALHFVANgTHSHCIKMVDKIMKNGFKL 169
Cdd:PHA03100  105 NGITPLLYAIS-KKSNSYSIVEYLLDNGANV 134
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 73-104 6.24e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 33.42  E-value: 6.24e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2416958208  73 DLRTPLLIAVE-LDDLEFVKSLIKSGANIDCID 104
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 73-102 7.94e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 32.94  E-value: 7.94e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 2416958208   73 DLRTPLLIAVELDDLEFVKSLIKSGANIDC 102
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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