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Conserved domains on  [gi|30690372|ref|NP_849499|]
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ankyrin repeat-containing protein 2 [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
185-298 3.24e-29

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 112.74  E-value: 3.24e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690372 185 HQTASLGDVEGLKAALASGGNKDEEDSEGRTALHFACGYGELKCAQVLIDAGASVNAVDKNKNTPLHYAAGYGRKECVSL 264
Cdd:COG0666  92 HAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKL 171

                        90       100       110
                ....*....|....*....|....*....|....
gi 30690372 265 LLENGAAVTLQNLDEKTPIDVAKLNSQLEVVKLL 298
Cdd:COG0666 172 LLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
STI1 pfam17830
STI1 domain; This entry corresponds to the STI1 domain that is found in two copies in the Sti1 ...
 102-156 9.89e-08

STI1 domain; This entry corresponds to the STI1 domain that is found in two copies in the Sti1 protein.


:

Pssm-ID: 436075  Cd Length: 55  Bit Score: 47.94  E-value: 9.89e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 30690372   102 SNPETAEhftermarMKEDPELKPILDEIDAGgPSAMMKYWNDPEVLKKLGEAMG 156
Cdd:pfam17830  10 ANPETRA--------LLSDPEFVAKLQQIQKN-PSSLQQYMQDPRVMTKLGVLMG 55
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
185-298 3.24e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 112.74  E-value: 3.24e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690372 185 HQTASLGDVEGLKAALASGGNKDEEDSEGRTALHFACGYGELKCAQVLIDAGASVNAVDKNKNTPLHYAAGYGRKECVSL 264
Cdd:COG0666  92 HAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKL 171

                        90       100       110
                ....*....|....*....|....*....|....
gi 30690372 265 LLENGAAVTLQNLDEKTPIDVAKLNSQLEVVKLL 298
Cdd:COG0666 172 LLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
Ank_2 pfam12796
Ankyrin repeats (3 copies);
185-276 6.10e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.47  E-value: 6.10e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690372   185 HQTASLGDVEGLKAALASGGNKDEEDSEGRTALHFACGYGELKCAQVLIDaGASVNAVDkNKNTPLHYAAGYGRKECVSL 264
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVKL 79

                          90
                  ....*....|..
gi 30690372   265 LLENGAAVTLQN 276
Cdd:pfam12796  80 LLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 187-298 6.60e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 68.54  E-value: 6.60e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690372  187 TASLGDVEGLKAALASGGNKDEEDSEGRTALHFA--CGYGELKCAQVLIDAGASVNA----------------VDKNKNT 248
Cdd:PHA03100 115 SKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYleSNKIDLKILKLLIDKGVDINAknrvnyllsygvpiniKDVYGFT 194

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 30690372  249 PLHYAAGYGRKECVSLLLENGAAVTLQNLDEKTPIDVAKLNSQLEVVKLL 298
Cdd:PHA03100 195 PLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLL 244
STI1 pfam17830
STI1 domain; This entry corresponds to the STI1 domain that is found in two copies in the Sti1 ...
 102-156 9.89e-08

STI1 domain; This entry corresponds to the STI1 domain that is found in two copies in the Sti1 protein.


Pssm-ID: 436075  Cd Length: 55  Bit Score: 47.94  E-value: 9.89e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 30690372   102 SNPETAEhftermarMKEDPELKPILDEIDAGgPSAMMKYWNDPEVLKKLGEAMG 156
Cdd:pfam17830  10 ANPETRA--------LLSDPEFVAKLQQIQKN-PSSLQQYMQDPRVMTKLGVLMG 55
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 245-274 4.81e-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: 39.49  E-value: 4.81e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 30690372    245 NKNTPLHYAAGYGRKECVSLLLENGAAVTL 274
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 208-269 3.19e-04

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: 42.05  E-value: 3.19e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30690372 208 EEDSEGRTALHFACGYGELKCAQVLIDAGASVNAV-------DKNKN-------TPLHYAAGYGRKECVSLLLENG 269
Cdd:cd22194 136 EEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHakgvffnPKYKHegfyfgeTPLALAACTNQPEIVQLLMEKE 211
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
185-298 3.24e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 112.74  E-value: 3.24e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690372 185 HQTASLGDVEGLKAALASGGNKDEEDSEGRTALHFACGYGELKCAQVLIDAGASVNAVDKNKNTPLHYAAGYGRKECVSL 264
Cdd:COG0666  92 HAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKL 171

                        90       100       110
                ....*....|....*....|....*....|....
gi 30690372 265 LLENGAAVTLQNLDEKTPIDVAKLNSQLEVVKLL 298
Cdd:COG0666 172 LLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
185-302 2.59e-27

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 107.73  E-value: 2.59e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690372 185 HQTASLGDVEGLKAALASGGNKDEEDSEGRTALHFACGYGELKCAQVLIDAGASVNAVDKNKNTPLHYAAGYGRKECVSL 264
Cdd:COG0666 125 HLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKL 204

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 30690372 265 LLENGAAVTLQNLDEKTPIDVAKLNSQLEVVKLLEKDA 302
Cdd:COG0666 205 LLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
127-298 2.76e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 94.25  E-value: 2.76e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690372 127 LDEIDAGGPSAMMKYWNDPEVLKKLGEAMGMPVAGLPDQTVSAEPEVAEEGEEEESIVHQTASLGDVEGLKAALASGGNK 206
Cdd:COG0666   1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690372 207 DEEDSEGRTALHFACGYGELKCAQVLIDAGASVNAVDKNKNTPLHYAAGYGRKECVSLLLENGAAVTLQNLDEKTPIDVA 286
Cdd:COG0666  81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                       170
                ....*....|..
gi 30690372 287 KLNSQLEVVKLL 298
Cdd:COG0666 161 AANGNLEIVKLL 172
Ank_2 pfam12796
Ankyrin repeats (3 copies);
185-276 6.10e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.47  E-value: 6.10e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690372   185 HQTASLGDVEGLKAALASGGNKDEEDSEGRTALHFACGYGELKCAQVLIDaGASVNAVDkNKNTPLHYAAGYGRKECVSL 264
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVKL 79

                          90
                  ....*....|..
gi 30690372   265 LLENGAAVTLQN 276
Cdd:pfam12796  80 LLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
185-304 8.65e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 87.32  E-value: 8.65e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690372 185 HQTASLGDVEGLKAALASGGNKDEEDSEGRTALHFACGYGELKCAQVLIDAGASVNAVDKNKNTPLHYAAGYGRKECVSL 264
Cdd:COG0666 158 HLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKL 237

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 30690372 265 LLENGAAVTLQNLDEKTPIDVAKLNSQLEVVKLLEKDAFL 304
Cdd:COG0666 238 LLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLL 277
Ank_2 pfam12796
Ankyrin repeats (3 copies);
217-302 1.53e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 73.23  E-value: 1.53e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690372   217 LHFACGYGELKCAQVLIDAGASVNAVDKNKNTPLHYAAGYGRKECVSLLLENgAAVTLQNlDEKTPIDVAKLNSQLEVVK 296
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78


                  ....*..
gi 30690372   297 -LLEKDA 302
Cdd:pfam12796  79 lLLEKGA 85
Ank_4 pfam13637
Ankyrin repeats (many copies);
213-266 1.91e-13

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 63.83  E-value: 1.91e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 30690372   213 GRTALHFACGYGELKCAQVLIDAGASVNAVDKNKNTPLHYAAGYGRKECVSLLL 266
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 187-298 6.60e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 68.54  E-value: 6.60e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690372  187 TASLGDVEGLKAALASGGNKDEEDSEGRTALHFA--CGYGELKCAQVLIDAGASVNA----------------VDKNKNT 248
Cdd:PHA03100 115 SKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYleSNKIDLKILKLLIDKGVDINAknrvnyllsygvpiniKDVYGFT 194

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 30690372  249 PLHYAAGYGRKECVSLLLENGAAVTLQNLDEKTPIDVAKLNSQLEVVKLL 298
Cdd:PHA03100 195 PLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLL 244
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 186-266 1.57e-12

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 67.62  E-value: 1.57e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690372  186 QTASLGDVEGLKAALASGGNKDEEDSEGRTALHFACGYGELKCAQVLIDAGASVNAVDKNKNTPLHYAAGYGRKECVSLL 265
Cdd:PTZ00322  88 QLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167


                 .
gi 30690372  266 L 266
Cdd:PTZ00322 168 S 168
PHA03095 PHA03095
ankyrin-like protein; Provisional
 192-298 9.18e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 65.05  E-value: 9.18e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690372  192 DVEGLKAALASGGNKDEEDSEGRTALH-FACGYGELKCAQVLIDAGASVNAVDKNKNTPLH-YAAGYGRKECV-SLLLEN 268
Cdd:PHA03095  62 VKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHvYLSGFNINPKViRLLLRK 141

                         90       100       110
                 ....*....|....*....|....*....|..
gi 30690372  269 GAAVTLQNLDEKTPIDV--AKLNSQLEVVKLL 298
Cdd:PHA03095 142 GADVNALDLYGMTPLAVllKSRNANVELLRLL 173
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 229-298 1.60e-11

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 64.92  E-value: 1.60e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690372  229 AQVLIDAGASVNAVDKNKNTPLHYAAGYGRKECVSLLLENGAAVTLQNLDEKTPIDVAKLNSQLEVVKLL 298
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 182-298 3.75e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 63.44  E-value: 3.75e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690372  182 SIVHQTASLGDVEGLKAALASGGNKDEEDSEGRTALHFACGYGELKCAQVLIDAGASVNAVDKNKNTPLHYAAGYGRKEC 261
Cdd:PHA02874 126 TFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYAC 205

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 30690372  262 VSLLLENGAAVTLQNLDEKTPIDVAKLNSQlEVVKLL 298
Cdd:PHA02874 206 IKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELL 241
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 192-298 1.97e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 61.05  E-value: 1.97e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690372  192 DVEGLKAALASGG--NKDEEDSeGRTALHFACGYGELKCAQVLIDAGASVNAVDKNKNTPLHYAAGYGRKECVSLLLENG 269
Cdd:PHA02878 146 EAEITKLLLSYGAdiNMKDRHK-GNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENG 224

                         90       100       110
                 ....*....|....*....|....*....|.
gi 30690372  270 AAVTLQNLDEKTP--IDVAKLNSqLEVVKLL 298
Cdd:PHA02878 225 ASTDARDKCGNTPlhISVGYCKD-YDILKLL 254
PHA03095 PHA03095
ankyrin-like protein; Provisional
 196-289 4.25e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 60.04  E-value: 4.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690372  196 LKAALASGGNKDEEDSEGRTALHFACGYGELKCAQV--LIDAGASVNAVDKNKNTPLHYAAGYGRKECVSLLLENGAAVT 273
Cdd:PHA03095 205 VRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADIN 284

                         90
                 ....*....|....*.
gi 30690372  274 LQNLDEKTPIDVAKLN 289
Cdd:PHA03095 285 AVSSDGNTPLSLMVRN 300
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 184-286 1.29e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 58.92  E-value: 1.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690372  184 VHQTASLGDVEGLKAALASGGNKDEEDSEGRTALHFA-CGYGELKCAQVLIDAGASVNAVDKNKNTPLHYAAGYGRK-EC 261
Cdd:PHA02876 379 IHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKlDV 458

                         90       100
                 ....*....|....*....|....*
gi 30690372  262 VSLLLENGAAVTLQNLDEKTPIDVA 286
Cdd:PHA02876 459 IEMLLDNGADVNAINIQNQYPLLIA 483
Ank_4 pfam13637
Ankyrin repeats (many copies);
247-298 7.87e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.12  E-value: 7.87e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 30690372   247 NTPLHYAAGYGRKECVSLLLENGAAVTLQNLDEKTPIDVAKLNSQLEVVKLL 298
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 225-296 8.07e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 56.61  E-value: 8.07e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30690372  225 ELKCAQVLIDAGASVNAVDKNKNTPLHYAAGYGRKECVSLLLENGAAVTLQNLDEKTPIDVAKLNSQLEVVK 296
Cdd:PHA02876 157 ELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIK 228
Ank_5 pfam13857
Ankyrin repeats (many copies);
232-286 8.41e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.81  E-value: 8.41e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 30690372   232 LIDAG-ASVNAVDKNKNTPLHYAAGYGRKECVSLLLENGAAVTLQNLDEKTPIDVA 286
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 182-298 6.98e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 53.35  E-value: 6.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690372  182 SIVHQTASLGDVEGLKAALASGGNKDEEDSEGRTALHFACGY-GELKCAQVLIDAGASVNAVDKNKN-TPLHYAAGYGRK 259
Cdd:PHA02878 203 SPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYILGlTALHSSIKSERK 282

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 30690372  260 ecVSLLLENGAAVTLQNLDEKTPIDVA-KLNSQLEVVKLL 298
Cdd:PHA02878 283 --LKLLLEYGADINSLNSYKLTPLSSAvKQYLCINIGRIL 320
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 182-304 9.52e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.04  E-value: 9.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690372  182 SIVHQTASLGDVEGLKAALASGGNKDEEDSEGRTALHFACGYGelKCAQVLIDAGASVNAVDKNKNTPLHYAAGYG-RKE 260
Cdd:PHA02874 192 SPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHN--RSAIELLINNASINDQDIDGSTPLHHAINPPcDID 269

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 30690372  261 CVSLLLENGAAVTLQNLDEKTPIDVA-KLNSQLEVVKLLEKDAFL 304
Cdd:PHA02874 270 IIDILLYHKADISIKDNKGENPIDTAfKYINKDPVIKDIIANAVL 314
STI1 pfam17830
STI1 domain; This entry corresponds to the STI1 domain that is found in two copies in the Sti1 ...
 102-156 9.89e-08

STI1 domain; This entry corresponds to the STI1 domain that is found in two copies in the Sti1 protein.


Pssm-ID: 436075  Cd Length: 55  Bit Score: 47.94  E-value: 9.89e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 30690372   102 SNPETAEhftermarMKEDPELKPILDEIDAGgPSAMMKYWNDPEVLKKLGEAMG 156
Cdd:pfam17830  10 ANPETRA--------LLSDPEFVAKLQQIQKN-PSSLQQYMQDPRVMTKLGVLMG 55
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 182-301 1.33e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 52.30  E-value: 1.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690372  182 SIVHQTASLGDVEGLKAALASGGNKDEEDSEGRTALHFACGYGELKCAQVLIDAGASVNAVDKNKN-TPLHYAAGYGRKE 260
Cdd:PHA02875 137 SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKID 216

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 30690372  261 CVSLLLENGA---AVTLQNLDEKTPIDVAK---LNSQLEVVKLLEKD 301
Cdd:PHA02875 217 IVRLFIKRGAdcnIMFMIEGEECTILDMICnmcTNLESEAIDALIAD 263
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 207-272 1.34e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 52.36  E-value: 1.34e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30690372  207 DEEDSEGRTALHFACGYGELKCAQVLIDAGASVNAVDKNKNTPLHYAAGYGRKECVSLLLENGAAV 272
Cdd:PHA03100 186 NIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSI 251
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
185-283 2.81e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 51.11  E-value: 2.81e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690372 185 HQTASLGDVEGLKAALASGGNKDEEDSEGRTALHFACGYGELKCAQVLIDAGASVNAVDKNKNTPLHYAAGYGRKECVSL 264
Cdd:COG0666 191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270

                        90
                ....*....|....*....
gi 30690372 265 LLENGAAVTLQNLDEKTPI 283
Cdd:COG0666 271 LLLALLLLAAALLDLLTLL 289
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 184-298 7.76e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 50.45  E-value: 7.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690372  184 VHQTASLGDVEGLKAALAS-GGNKDEEDSEGRTALHFACGYGELKCAQVLIDAGASVNAVDKNKNTPLHYA-AGYGRKEC 261
Cdd:PHA02876 345 LHQASTLDRNKDIVITLLElGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMS 424

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 30690372  262 VSLLLENGAAVTLQNLDEKTPIDVA-KLNSQLEVVKLL 298
Cdd:PHA02876 425 VKTLIDRGANVNSKNKDLSTPLHYAcKKNCKLDVIEML 462
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 188-298 8.95e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 50.25  E-value: 8.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690372  188 ASLGDVEGLKAALASGGNKDEEDSEGRTALHFACGYGELKCAQVLIDAGASVNAVDKNKNTPL-------HY-------- 252
Cdd:PLN03192 533 ASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnaisakHHkifrilyh 612

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30690372  253 ----------------AAGYGRKECVSLLLENGAAVTLQNLDEKTPIDVAKLNSQLEVVKLL 298
Cdd:PLN03192 613 fasisdphaagdllctAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLL 674
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 190-300 9.66e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 49.60  E-value: 9.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690372  190 LGDVEGLKAALASGGNKDEEDSEGRTALHFACGYGELKCAQVLIDAGASVNAV-DKNKNTPLHYAAGYGRKECVSLLLEN 268
Cdd:PHA02875  45 FRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVfYKDGMTPLHLATILKKLDIMKLLIAR 124

                         90       100       110
                 ....*....|....*....|....*....|..
gi 30690372  269 GAAVTLQNLDEKTPIDVAKLNSQLEVVKLLEK 300
Cdd:PHA02875 125 GADPDIPNTDKFSPLHLAVMMGDIKGIELLID 156
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 212-244 1.23e-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. 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: 44.20  E-value: 1.23e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 30690372   212 EGRTALHFACG-YGELKCAQVLIDAGASVNAVDK 244
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 192-283 1.31e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 49.68  E-value: 1.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690372  192 DVEGLKAALASGGNKDEEDsegrTALHFACGYGELKCAQVLIDAGASVNAVDKNKNTPLHYAAGY-GRKECVSLLLENGA 270
Cdd:PHA02876 223 NIDTIKAIIDNRSNINKND----LSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQApSLSRLVPKLLERGA 298

                         90
                 ....*....|...
gi 30690372  271 AVTLQNLDEKTPI 283
Cdd:PHA02876 299 DVNAKNIKGETPL 311
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 184-300 1.73e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 48.83  E-value: 1.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690372  184 VHQTASLGDVEGLKAALASGGNKDEEDSEGRTALHFACGYGELKCAQVLIDAGASVNAVDKNKNTPLHYAAGYGRKECVS 263
Cdd:PHA02875 106 LHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICK 185

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 30690372  264 LLLENGAAVtlqNLDEKTPiDVAKL-----NSQLEVVKLLEK 300
Cdd:PHA02875 186 MLLDSGANI---DYFGKNG-CVAALcyaieNNKIDIVRLFIK 223
Ank_5 pfam13857
Ankyrin repeats (many copies);
209-253 1.76e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.26  E-value: 1.76e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 30690372   209 EDSEGRTALHFACGYGELKCAQVLIDAGASVNAVDKNKNTPLHYA 253
Cdd:pfam13857  12 LDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03095 PHA03095
ankyrin-like protein; Provisional
 192-286 2.04e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 48.87  E-value: 2.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690372  192 DVEGLKAALASGGNKDEEDSEGRTALHFACGY--GELKCAQVLIDAGASVNAVDKNKNTPLHYAAGYG--RKECVSLLLE 267
Cdd:PHA03095 166 NVELLRLLIDAGADVYAVDDRFRSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSscKRSLVLPLLI 245

                         90
                 ....*....|....*....
gi 30690372  268 NGAAVTLQNLDEKTPIDVA 286
Cdd:PHA03095 246 AGISINARNRYGQTPLHYA 264
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 245-276 4.07e-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. 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: 42.66  E-value: 4.07e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 30690372   245 NKNTPLHYAAG-YGRKECVSLLLENGAAVTLQN 276
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 196-298 4.20e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 47.74  E-value: 4.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690372  196 LKAALASGGNKDEEDSEGRTALHFACGYG-----ELKCAQVLIDAGASVNAVDKNKNTPLHYAAGY--GRKECVSLLLEN 268
Cdd:PHA03100  51 VKILLDNGADINSSTKNNSTPLHYLSNIKynltdVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDN 130

                         90       100       110
                 ....*....|....*....|....*....|..
gi 30690372  269 GAAVTLQNLDEKTPIDVA-KLNS-QLEVVKLL 298
Cdd:PHA03100 131 GANVNIKNSDGENLLHLYlESNKiDLKILKLL 162
Ank_4 pfam13637
Ankyrin repeats (many copies);
182-233 1.27e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.88  E-value: 1.27e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 30690372   182 SIVHQTASLGDVEGLKAALASGGNKDEEDSEGRTALHFACGYGELKCAQVLI 233
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 232-298 1.35e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.17  E-value: 1.35e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30690372  232 LIDAGASVNAVDKNKNTPLHYAAGYG---RKECVSLLLENGAAVTLQNLDEKTPIDVAKLNSQ-LEVVKLL 298
Cdd:PHA03095  33 LLAAGADVNFRGEYGKTPLHLYLHYSsekVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLL 103
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 245-274 4.81e-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: 39.49  E-value: 4.81e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 30690372    245 NKNTPLHYAAGYGRKECVSLLLENGAAVTL 274
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 245-272 5.42e-05

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.55  E-value: 5.42e-05
                          10        20
                  ....*....|....*....|....*...
gi 30690372   245 NKNTPLHYAAGYGRKECVSLLLENGAAV 272
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
PHA02946 PHA02946
ankyin-like protein; Provisional
 200-280 1.24e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 43.12  E-value: 1.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690372  200 LASGGNKDEEDSEGRTALHFACGYGELKCAQVLIDAGASVNAVDKNKNTPLHYAAGYGRK--ECVSLLLENGAAVTlQNL 277
Cdd:PHA02946  59 LHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEviERINLLVQYGAKIN-NSV 137


                 ...
gi 30690372  278 DEK 280
Cdd:PHA02946 138 DEE 140
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 212-241 1.47e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.34  E-value: 1.47e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 30690372    212 EGRTALHFACGYGELKCAQVLIDAGASVNA 241
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 182-298 1.53e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 43.06  E-value: 1.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690372  182 SIVHQTASLGDVEGLKAALASGGNKDEE-DSEGRTALHFACGYGELKCAQVLIDAGASVNAVDKNKNTPLHYAAGYGRKE 260
Cdd:PHA02875  70 SELHDAVEEGDVKAVEELLDLGKFADDVfYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIK 149

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 30690372  261 CVSLLLENGAAVTLQNLDEKTPIDVAKLNSQLEVVKLL 298
Cdd:PHA02875 150 GIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKML 187
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 212-241 3.08e-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: 37.24  E-value: 3.08e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 30690372   212 EGRTALHFACGYGELKCAQVLIDAGASVNA 241
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 208-269 3.19e-04

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: 42.05  E-value: 3.19e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30690372 208 EEDSEGRTALHFACGYGELKCAQVLIDAGASVNAV-------DKNKN-------TPLHYAAGYGRKECVSLLLENG 269
Cdd:cd22194 136 EEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHakgvffnPKYKHegfyfgeTPLALAACTNQPEIVQLLMEKE 211
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 223-298 4.78e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 40.57  E-value: 4.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690372  223 YGELKCAQVLIDAGASVNAVDKNKN-TPLHYAAGYGRK---ECVSLLLENGAAVTLQNLDEKTPIDV--AKLNSQLEVVK 296
Cdd:PHA02859  63 KVNVEILKFLIENGADVNFKTRDNNlSALHHYLSFNKNvepEILKILIDSGSSITEEDEDGKNLLHMymCNFNVRINVIK 142


                 ..
gi 30690372  297 LL 298
Cdd:PHA02859 143 LL 144
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 196-270 5.72e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 41.59  E-value: 5.72e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30690372  196 LKAALASGGNKDEEDSEGRTALHFACGYG-ELKCAQVLIDAGASVNAVDKNKNTPLHYAAGYgrKECVSLLLENGA 270
Cdd:PHA02876 425 VKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIALEY--HGIVNILLHYGA 498
PHA02741 PHA02741
hypothetical protein; Provisional
 210-300 6.50e-04

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 39.64  E-value: 6.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690372  210 DSEGRTALHFACGYGE----LKCAQVLIDAGASVNAVDK-NKNTPLHYAAGYGRKECVSLLL-ENGAAVTLQNLDEKTPI 283
Cdd:PHA02741  57 DDAGQMCIHIAAEKHEaqlaAEIIDHLIELGADINAQEMlEGDTALHLAAHRRDHDLAEWLCcQPGIDLHFCNADNKSPF 136

                         90
                 ....*....|....*..
gi 30690372  284 DVAKLNSQLEVVKLLEK 300
Cdd:PHA02741 137 ELAIDNEDVAMMQILRE 153
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 188-243 7.92e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.01  E-value: 7.92e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 30690372  188 ASLGDVEGLKAALASGGNKDEEDSEGRTALHFACGYGELKCAQVLIDAGASVNAVD 243
Cdd:PLN03192 630 AKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
PHA02798 PHA02798
ankyrin-like protein; Provisional
 226-298 2.30e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 39.43  E-value: 2.30e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30690372  226 LKCAQVLIDAGASVNAVDKNKNTPLH--YAAGY-GRKECVSLLLENGAAVTLQNLDEKTPIDV---AKLNSQLEVVKLL 298
Cdd:PHA02798  89 LDIVKILIENGADINKKNSDGETPLYclLSNGYiNNLEILLFMIENGADTTLLDKDGFTMLQVylqSNHHIDIEIIKLL 167
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 215-286 2.31e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 39.20  E-value: 2.31e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30690372  215 TALHFACGYGELKCAQVLIDAGASVNA-VDKNKNTPLHYAAGYGRKECVSLLLENGAAVTLQNLDEKTPIDVA 286
Cdd:PHA02884  72 NPLIYAIDCDNDDAAKLLIRYGADVNRyAEEAKITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELA 144
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 212-275 2.70e-03

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: 39.23  E-value: 2.70e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30690372 212 EGRTALHFACGYGELKCAQVLIDAGASVN-------AVDKNKNT-------PLHYAAGYGRKECVSLLLENGAAVTLQ 275
Cdd:cd22192  88 QGETALHIAVVNQNLNLVRELIARGADVVspratgtFFRPGPKNliyygehPLSFAACVGNEEIVRLLIEHGADIRAQ 165
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 191-300 2.74e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 39.18  E-value: 2.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690372  191 GDVEGLKAALASGGN-KDEEDSEGRTALHFACGYGELKCAQVLIDAGASVNAVDKNKNTPLHYAAGYGRKECVSLLLENG 269
Cdd:PHA02874  12 GDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG 91

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 30690372  270 A-----------------------AVTLQNLDEKTPIDVAKLNSQLEVVKLLEK 300
Cdd:PHA02874  92 VdtsilpipciekdmiktildcgiDVNIKDAELKTFLHYAIKKGDLESIKMLFE 145
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 208-290 4.60e-03

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: 38.62  E-value: 4.60e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690372 208 EEDSEGRTALHFACGYGELKCAQVLIDAGASVNAVDKNK--------------NTPLHYAAGYGRKECVSLLLENgaavt 273
Cdd:cd22193  71 DEYYEGQTALHIAIERRQGDIVALLVENGADVHAHAKGRffqpkyqgegfyfgELPLSLAACTNQPDIVQYLLEN----- 145

                        90
                ....*....|....*..
gi 30690372 274 lqnldEKTPIDVAKLNS 290
Cdd:cd22193 146 -----EHQPADIEAQDS 157
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 212-270 4.77e-03

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 38.32  E-value: 4.77e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30690372 212 EGRTALHFACGYGELKCAQVLIDAGASVNA------VDKNKNT-------PLHYAAGYGRKECVSLLLENGA 270
Cdd:cd21882  72 QGQTALHIAIENRNLNLVRLLVENGADVSAratgrfFRKSPGNlfyfgelPLSLAACTNQEEIVRLLLENGA 143
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 192-289 4.83e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 37.49  E-value: 4.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690372  192 DVEGLKAALASGGNKDEEDSEGRTALH-FACGYG-ELKCAQVLIDAGASVNAVDKNKNTPLH-YAAGYGRKECVSLLLEN 268
Cdd:PHA02859 102 EPEILKILIDSGSSITEEDEDGKNLLHmYMCNFNvRINVIKLLIDSGVSFLNKDFDNNNILYsYILFHSDKKIFDFLTSL 181

                         90       100
                 ....*....|....*....|.
gi 30690372  269 GAAVTLQNLDEKTPIDVAKLN 289
Cdd:PHA02859 182 GIDINETNKSGYNCYDLIKFR 202
PHA02917 PHA02917
ankyrin-like protein; Provisional
 239-298 5.71e-03

ankyrin-like protein; Provisional


Pssm-ID: 165231 [Multi-domain]  Cd Length: 661  Bit Score: 38.44  E-value: 5.71e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30690372  239 VNAVDKNKNTPLHYAAGYGRKECVSLLLENGAAVTLQNLDEKTPIDVAKLNSQ-LEVVKLL 298
Cdd:PHA02917 445 INMIDKRGETLLHKAVRYNKQSLVSLLLESGSDVNIRSNNGYTCIAIAINESRnIELLKML 505
PHA02798 PHA02798
ankyrin-like protein; Provisional
 226-283 7.93e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 37.51  E-value: 7.93e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30690372  226 LKCAQVLIDAGASVNAVDKNKNTPL----HYAAGYGRK-ECVSLLLENGAAVTLQNLDEKTPI 283
Cdd:PHA02798  51 TDIVKLFINLGANVNGLDNEYSTPLctilSNIKDYKHMlDIVKILIENGADINKKNSDGETPL 113
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 208-298 8.16e-03

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 37.55  E-value: 8.16e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690372 208 EEDSEGRTALHFACGY---GELKCAQVLIDAGASVNAVDKNKNTP-----------LHYAAGYGRKECVSLLLENGAAVT 273
Cdd:cd21882  21 QRGATGKTCLHKAALNlndGVNEAIMLLLEAAPDSGNPKELVNAPctdefyqgqtaLHIAIENRNLNLVRLLVENGADVS 100

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 30690372 274 LQ---NLDEKT----------PIDVAKLNSQLEVVKLL 298
Cdd:cd21882 101 ARatgRFFRKSpgnlfyfgelPLSLAACTNQEEIVRLL 138
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 200-303 8.67e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 37.74  E-value: 8.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690372  200 LASGGNKDEEDSEGRTALHFACGYGELKCAQVLIDAGASVNAVDKNKNTPLHYAAGYGRKECVSLLLENGAAVTLQNLDE 279
Cdd:PHA02876 165 LEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNDLSL 244

                         90       100
                 ....*....|....*....|....
gi 30690372  280 KTPIDvaklNSQLEVVKLLEKDAF 303
Cdd:PHA02876 245 LKAIR----NEDLETSLLLYDAGF 264
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 186-272 9.84e-03

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: 37.30  E-value: 9.84e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690372 186 QTASLGDVEGLKAALASGG-NKDEEDSEGRTALHFACGYGELKCAQVLIDAGAS-VNAVDKNK----NTPLHYAAGYGRK 259
Cdd:cd22192  23 LAAKENDVQAIKKLLKCPScDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPMTSDlyqgETALHIAVVNQNL 102

                        90
                ....*....|...
gi 30690372 260 ECVSLLLENGAAV 272
Cdd:cd22192 103 NLVRELIARGADV 115
 
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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