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Conserved domains on  [gi|1240296434|ref|NP_001342037|]
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GA-binding protein subunit beta-1 isoform g [Mus musculus]

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];
10-92 7.55e-20

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 87.70  E-value: 7.55e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240296434  10 LLEAARAGQDDEVRILMANGA-PFTTDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVE 88
Cdd:COG0666   124 LHLAAYNGNLEIVKLLLEAGAdVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK 203


                  ....
gi 1240296434  89 VLLK 92
Cdd:COG0666   204 LLLE 207
Oberon_cc super family cl24780
Coiled-coil region of Oberon; Oberon_cc is the coiled-coil region of Oberon proteins from ...
 251-305 5.55e-03

Coiled-coil region of Oberon; Oberon_cc is the coiled-coil region of Oberon proteins from plants. Oberon is necessary for maintenance and/or establishment of both the shoot and root apical meristems in Arabidopsis. Most Oberon proteins carry a PHD finger domain, pfam07227 and this coiled-coil domain. Oberon proteins mediate the TMO7 (the direct target of MP) expression through modification of, or binding to, chromatin at the TMO7 locus. TMO7 stands for the target of Monopteros 7 (or Auxin response factor 7).


The actual alignment was detected with superfamily member pfam16312:

Pssm-ID: 465089 [Multi-domain]  Cd Length: 129  Bit Score: 36.50  E-value: 5.55e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1240296434 251 KRQCMEIIESRVECAEIEErEALQKQLDEANREAQKYRQQLLKKE----------------QEAEAYRQKL 305
Cdd:pfam16312  31 KKQQIEELESIVRLKQAEA-EMFQLKADEARREAEGLQRIALAKSekseeeyasrylklrlEEAEEERRYK 100
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
10-92 7.55e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 87.70  E-value: 7.55e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240296434  10 LLEAARAGQDDEVRILMANGA-PFTTDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVE 88
Cdd:COG0666   124 LHLAAYNGNLEIVKLLLEAGAdVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK 203


                  ....
gi 1240296434  89 VLLK 92
Cdd:COG0666   204 LLLE 207
Ank_2 pfam12796
Ankyrin repeats (3 copies);
10-92 9.72e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.60  E-value: 9.72e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240296434  10 LLEAARAGQDDEVRILMANGA-PFTTDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDarTKVDRTPLHMAASEGHANIVE 88
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGAdANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78


                  ....
gi 1240296434  89 VLLK 92
Cdd:pfam12796  79 LLLE 82
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 6-92 1.16e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.98  E-value: 1.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240296434   6 LGKKLLEAARAGQDDEVRILMANGA-PFTTDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHA 84
Cdd:PTZ00322   82 LTVELCQLAASGDAVGARILLTGGAdPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFR 161


                  ....*...
gi 1240296434  85 NIVEVLLK 92
Cdd:PTZ00322  162 EVVQLLSR 169
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 71-92 5.74e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.80  E-value: 5.74e-04
                           10        20
                   ....*....|....*....|..
gi 1240296434   71 DRTPLHMAASEGHANIVEVLLK 92
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLD 23
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 10-92 2.39e-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: 39.61  E-value: 2.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240296434  10 LLEAARAGQDDEVRILMANGA--PFTTDWLGTSPLHLAAQYGHFSTTEVLLRAgvsrdARTKVD----------RTPLHM 77
Cdd:cd22192    21 LLLAAKENDVQAIKKLLKCPScdLFQRGALGETALHVAALYDNLEAAVVLMEA-----APELVNepmtsdlyqgETALHI 95

                          90
                  ....*....|....*
gi 1240296434  78 AASEGHANIVEVLLK 92
Cdd:cd22192    96 AVVNQNLNLVRELIA 110
Oberon_cc pfam16312
Coiled-coil region of Oberon; Oberon_cc is the coiled-coil region of Oberon proteins from ...
 251-305 5.55e-03

Coiled-coil region of Oberon; Oberon_cc is the coiled-coil region of Oberon proteins from plants. Oberon is necessary for maintenance and/or establishment of both the shoot and root apical meristems in Arabidopsis. Most Oberon proteins carry a PHD finger domain, pfam07227 and this coiled-coil domain. Oberon proteins mediate the TMO7 (the direct target of MP) expression through modification of, or binding to, chromatin at the TMO7 locus. TMO7 stands for the target of Monopteros 7 (or Auxin response factor 7).


Pssm-ID: 465089 [Multi-domain]  Cd Length: 129  Bit Score: 36.50  E-value: 5.55e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1240296434 251 KRQCMEIIESRVECAEIEErEALQKQLDEANREAQKYRQQLLKKE----------------QEAEAYRQKL 305
Cdd:pfam16312  31 KKQQIEELESIVRLKQAEA-EMFQLKADEARREAEGLQRIALAKSekseeeyasrylklrlEEAEEERRYK 100
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
10-92 7.55e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 87.70  E-value: 7.55e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240296434  10 LLEAARAGQDDEVRILMANGA-PFTTDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVE 88
Cdd:COG0666   124 LHLAAYNGNLEIVKLLLEAGAdVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK 203


                  ....
gi 1240296434  89 VLLK 92
Cdd:COG0666   204 LLLE 207
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
10-92 6.25e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 85.01  E-value: 6.25e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240296434  10 LLEAARAGQDDEVRILMANGA-PFTTDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVE 88
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGAdVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170


                  ....
gi 1240296434  89 VLLK 92
Cdd:COG0666   171 LLLE 174
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
10-102 4.77e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 76.92  E-value: 4.77e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240296434  10 LLEAARAGQDDEVRILMANGA-PFTTDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVE 88
Cdd:COG0666   157 LHLAAANGNLEIVKLLLEAGAdVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVK 236

                          90
                  ....*....|....
gi 1240296434  89 VLLKIAMQNQINTN 102
Cdd:COG0666   237 LLLEAGADLNAKDK 250
Ank_2 pfam12796
Ankyrin repeats (3 copies);
10-92 9.72e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.60  E-value: 9.72e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240296434  10 LLEAARAGQDDEVRILMANGA-PFTTDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDarTKVDRTPLHMAASEGHANIVE 88
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGAdANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78


                  ....
gi 1240296434  89 VLLK 92
Cdd:pfam12796  79 LLLE 82
Ank_2 pfam12796
Ankyrin repeats (3 copies);
42-97 4.37e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 61.29  E-value: 4.37e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1240296434  42 LHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVEVLLKIAMQN 97
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN 56
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
10-141 4.14e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 62.66  E-value: 4.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240296434  10 LLEAARAGQDDEVRILMANGAP-FTTDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVE 88
Cdd:COG0666    58 LLAAALAGDLLVALLLLAAGADiNAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1240296434  89 VLLK----IAMQNQINTNP-------ESPDTVtihaatpQFIIGPGGVVNLTDETGVS----AVQFGN 141
Cdd:COG0666   138 LLLEagadVNAQDNDGNTPlhlaaanGNLEIV-------KLLLEAGADVNARDNDGETplhlAAENGH 198
Ank_4 pfam13637
Ankyrin repeats (many copies);
38-91 2.80e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.28  E-value: 2.80e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1240296434  38 GTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVEVLL 91
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
10-94 8.13e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 55.73  E-value: 8.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240296434  10 LLEAARAGQDDEVRILMANGA-PFTTDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVE 88
Cdd:COG0666   190 LHLAAENGHLEIVKLLLEAGAdVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVK 269


                  ....*.
gi 1240296434  89 VLLKIA 94
Cdd:COG0666   270 LLLLAL 275
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 6-92 1.16e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.98  E-value: 1.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240296434   6 LGKKLLEAARAGQDDEVRILMANGA-PFTTDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHA 84
Cdd:PTZ00322   82 LTVELCQLAASGDAVGARILLTGGAdPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFR 161


                  ....*...
gi 1240296434  85 NIVEVLLK 92
Cdd:PTZ00322  162 EVVQLLSR 169
PHA03095 PHA03095
ankyrin-like protein; Provisional
 20-92 1.18e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.56  E-value: 1.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240296434  20 DEVRILMANGAPF-TTDWLGTSPLHLaaqYGHFSTTE----VLLRAGVSRDARTKVDRTPLHMAAS--EGHANIVEVLLK 92
Cdd:PHA03095   64 DIVRLLLEAGADVnAPERCGFTPLHL---YLYNATTLdvikLLIKAGADVNAKDKVGRTPLHVYLSgfNINPKVIRLLLR 140
Ank_2 pfam12796
Ankyrin repeats (3 copies);
10-63 2.99e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 42.03  E-value: 2.99e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1240296434  10 LLEAARAGQDDEVRILMANGAPFTTDwLGTSPLHLAAQYGHFSTTEVLLRAGVS 63
Cdd:pfam12796  34 LHLAAKNGHLEIVKLLLEHADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGAD 86
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
10-141 3.17e-05

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 44.94  E-value: 3.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240296434  10 LLEAARAGQDDEVRILMANGAPFTTDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVEV 89
Cdd:COG0666    26 LAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKL 105

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240296434  90 LLK-IAMQNQINTNPESPDTVTI---HAATPQFIIGPGGVVNLTDETGVS----AVQFGN 141
Cdd:COG0666   106 LLEaGADVNARDKDGETPLHLAAyngNLEIVKLLLEAGADVNAQDNDGNTplhlAAANGN 165
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 34-92 5.62e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 44.86  E-value: 5.62e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1240296434  34 TDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVEVLLK 92
Cdd:PLN03192  521 DDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLK 579
Ank_4 pfam13637
Ankyrin repeats (many copies);
10-58 1.19e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.18  E-value: 1.19e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1240296434  10 LLEAARAGQDDEVRILMANGAPF-TTDWLGTSPLHLAAQYGHFSTTEVLL 58
Cdd:pfam13637   5 LHAAAASGHLELLRLLLEKGADInAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 22-79 1.54e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 43.09  E-value: 1.54e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1240296434  22 VRILMANGA-PFTTDWLGTSPLHLAAQYGHFSTTEV--LLRAGVSRDARTKVDRTPLHMAA 79
Cdd:PHA03095  205 VRELIRAGCdPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAA 265
Ank_5 pfam13857
Ankyrin repeats (many copies);
30-78 1.79e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.87  E-value: 1.79e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1240296434  30 APFTTDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMA 78
Cdd:pfam13857   8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 13-106 1.84e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 43.03  E-value: 1.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240296434  13 AARAGQDDEVRILMANGAPFTT-DWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHAnIVEVLL 91
Cdd:PHA02874  164 AIKHNFFDIIKLLLEKGAYANVkDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRS-AIELLI 242

                          90
                  ....*....|....*
gi 1240296434  92 KIAMQNQINTNPESP 106
Cdd:PHA02874  243 NNASINDQDIDGSTP 257
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 14-91 1.95e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 43.13  E-value: 1.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240296434  14 ARAGQDDE-VRILMANGAPFT-TDWLGTSPLHLAAQYGHFSTTEV-LLRAGVSRDARTKVDRTPLHMAASEGHANIVEVL 90
Cdd:PHA02876  315 AKNGYDTEnIRTLIMLGADVNaADRLYITPLHQASTLDRNKDIVItLLELGANVNARDYCDKTPIHYAAVRNNVVIINTL 394


                  .
gi 1240296434  91 L 91
Cdd:PHA02876  395 L 395
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 71-92 5.74e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.80  E-value: 5.74e-04
                           10        20
                   ....*....|....*....|..
gi 1240296434   71 DRTPLHMAASEGHANIVEVLLK 92
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLD 23
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 38-69 8.08e-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. 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: 36.50  E-value: 8.08e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1240296434  38 GTSPLHLAA-QYGHFSTTEVLLRAGVSRDARTK 69
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 22-102 1.92e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 39.86  E-value: 1.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240296434  22 VRILMANGAPFT--TDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVEVLLkiamQNQI 99
Cdd:PHA02878  150 TKLLLSYGADINmkDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILL----ENGA 225


                  ...
gi 1240296434 100 NTN 102
Cdd:PHA02878  226 STD 228
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 10-92 2.39e-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: 39.61  E-value: 2.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240296434  10 LLEAARAGQDDEVRILMANGA--PFTTDWLGTSPLHLAAQYGHFSTTEVLLRAgvsrdARTKVD----------RTPLHM 77
Cdd:cd22192    21 LLLAAKENDVQAIKKLLKCPScdLFQRGALGETALHVAALYDNLEAAVVLMEA-----APELVNepmtsdlyqgETALHI 95

                          90
                  ....*....|....*
gi 1240296434  78 AASEGHANIVEVLLK 92
Cdd:cd22192    96 AVVNQNLNLVRELIA 110
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 20-92 5.52e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 38.11  E-value: 5.52e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1240296434  20 DEVRILMANGAPF-TTDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVEVLLK 92
Cdd:PHA03100  173 NRVNYLLSYGVPInIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLN 246
Oberon_cc pfam16312
Coiled-coil region of Oberon; Oberon_cc is the coiled-coil region of Oberon proteins from ...
 251-305 5.55e-03

Coiled-coil region of Oberon; Oberon_cc is the coiled-coil region of Oberon proteins from plants. Oberon is necessary for maintenance and/or establishment of both the shoot and root apical meristems in Arabidopsis. Most Oberon proteins carry a PHD finger domain, pfam07227 and this coiled-coil domain. Oberon proteins mediate the TMO7 (the direct target of MP) expression through modification of, or binding to, chromatin at the TMO7 locus. TMO7 stands for the target of Monopteros 7 (or Auxin response factor 7).


Pssm-ID: 465089 [Multi-domain]  Cd Length: 129  Bit Score: 36.50  E-value: 5.55e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1240296434 251 KRQCMEIIESRVECAEIEErEALQKQLDEANREAQKYRQQLLKKE----------------QEAEAYRQKL 305
Cdd:pfam16312  31 KKQQIEELESIVRLKQAEA-EMFQLKADEARREAEGLQRIALAKSekseeeyasrylklrlEEAEEERRYK 100
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 20-115 6.13e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 38.11  E-value: 6.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240296434  20 DEVRILMANGA-PFTTDWLGTSPLHLAAQYGHFST-----TEVLLRAGVSRDARTKVDRTPLHMAASE--GHANIVEVLL 91
Cdd:PHA03100   49 DVVKILLDNGAdINSSTKNNSTPLHYLSNIKYNLTdvkeiVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLL 128

                          90       100
                  ....*....|....*....|....*
gi 1240296434  92 kiamQNQINTNPESPDTVT-IHAAT 115
Cdd:PHA03100  129 ----DNGANVNIKNSDGENlLHLYL 149
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 5-92 6.26e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 38.05  E-value: 6.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240296434   5 DLGKKLLEAARAGQDDEVRILMANGApFTTDWL---GTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASE 81
Cdd:PHA02875   67 DIESELHDAVEEGDVKAVEELLDLGK-FADDVFykdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMM 145

                          90
                  ....*....|.
gi 1240296434  82 GHANIVEVLLK 92
Cdd:PHA02875  146 GDIKGIELLID 156
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 5-105 7.03e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 37.94  E-value: 7.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240296434   5 DLGKKLLEAARAGQD-DEVRILMANGA-PFTTDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAAseG 82
Cdd:PHA02878  166 HKGNTALHYATENKDqRLTELLLSYGAnVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISV--G 243

                          90       100
                  ....*....|....*....|...
gi 1240296434  83 HANIVEVlLKIAMQNQINTNPES 105
Cdd:PHA02878  244 YCKDYDI-LKLLLEHGVDVNAKS 265
CREPT pfam16566
Cell-cycle alteration and expression-elevated protein in tumour; CREPT (Cell-cycle alteration ...
 265-313 7.10e-03

Cell-cycle alteration and expression-elevated protein in tumour; CREPT (Cell-cycle alteration and expression-elevated protein in tumour) is a family of eukaryotic transcriptional regulators that ptromote the binding of RNA-polymerase to the CYCLIN D1, CCDN1, promoter and other genes involved in the cell-cycle. It promotes the formation of a chromatin loop in the CYCLIN D1 gene, and is preferentially expressed in a range of different human tumours.


Pssm-ID: 465181 [Multi-domain]  Cd Length: 147  Bit Score: 36.44  E-value: 7.10e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1240296434 265 AEIEEREALQKQLDEAnreAQKYRQQLLKKEQEAEAYRQKLEAMTRIQT 313
Cdd:pfam16566  69 AELEDRKKVAQMLRDF---LQLQKELLAQAEERLEEYKEKLEKVSQVRK 114
Stathmin pfam00836
Stathmin family; The Stathmin family of proteins play an important role in the regulation of ...
 229-306 8.39e-03

Stathmin family; The Stathmin family of proteins play an important role in the regulation of the microtubule cytoskeleton. They regulate microtubule dynamics by promoting depolymerization of microtubules and/or preventing polymerization of tubulin heterodimers.


Pssm-ID: 459956 [Multi-domain]  Cd Length: 136  Bit Score: 36.17  E-value: 8.39e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1240296434 229 QVLTVPATDIAEETVISEEPPAKRQCMEIIESRVECAEiEEREALqkqldeanrEAQKYRQQLLKKEQEAEAYRQKLE 306
Cdd:pfam00836  18 EVILKPPSVNAAPPKLSLSPKKKDSSLEEIQKKLEAAE-ERRKSL---------EAQKLKQLAEKREKEEEALQKADE 85
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 72-92 9.19e-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: 9.19e-03
                          10        20
                  ....*....|....*....|..
gi 1240296434  72 RTPLHMAA-SEGHANIVEVLLK 92
Cdd:pfam00023   3 NTPLHLAAgRRGNLEIVKLLLS 24
 
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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