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Conserved domains on  [gi|2462553036|ref|XP_054171004|]
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ankyrin repeat domain-containing protein 13B isoform X2 [Homo sapiens]

Protein Classification

GPCR_chapero_1 domain-containing protein( domain architecture ID 12790908)

GPCR_chapero_1 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GPCR_chapero_1 pfam11904
GPCR-chaperone; This domain, and the associated ANK family repeat pfam00023 domain, together ...
 155-493 4.91e-137

GPCR-chaperone; This domain, and the associated ANK family repeat pfam00023 domain, together act as a chaperone for biogenesis and folding of the DP receptor for prostaglandin D2.


:

Pssm-ID: 463391  Cd Length: 298  Bit Score: 402.01  E-value: 4.91e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462553036 155 RVDTTLLGFDHMTWQRGNRSFVFRGQDTS-AVVMEIDHDRRVVYTETLALAGQDRElllaaaqpTEEQVLSRLTAPVVTT 233
Cdd:pfam11904   1 RADTTLLGFDGFKWQRGDQSFLFLGDGDSpGSLLELDHDEKEVQLEGAGAEASEEE--------VEEEVAARLQTPIVRP 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462553036 234 QLDTKNISFERNKTGilgW-RSEKTEMVNGYEAKVYGASNVELITRTRTEHLSEQHKGKVK-------GCKTPLQSFLGI 305
Cdd:pfam11904  73 GIDVTKISFERNKSG---WrRQEKTEMVGGYKAKVYDASNVELSTKSRTEHLSEEEKAKLKsaleppeGSRTPLQSFLGI 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462553036 306 AEQHGGPQNGTLITQTLSQANPTAITAEEYFNPnfelgnrdmgrPMELTTKTQnvpyplgsgggRFKAKLWLCEEHPLSL 385
Cdd:pfam11904 150 AEEEKGWFGKTREESEAPPTNPTALTPEEYFDP-----------PKEESEKKK-----------GFKATLWLSEDFPLSL 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462553036 386 cEQVAPIIDLMAVSNALFAKLRDFITLRLPPGFPVKIEIPIFHILNARITFGNLNGCDePVPSVRGSPSSETPSPGsdss 465
Cdd:pfam11904 208 -EQLLPILDLLANKVKHFRRLREFITLKLPPGFPVKIEIPVFPTVNARITFTKFEELD-PVEEFSTPIKSPERGSP---- 281

                         330       340
                  ....*....|....*....|....*...
gi 2462553036 466 svsssssttscRGCEISPALFEAPRGYS 493
Cdd:pfam11904 282 -----------SSCEIDDDPFEIPSGYT 298
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
32-95 1.08e-13

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 71.91  E-value: 1.08e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462553036  32 DIEQLDPRGRTPLHLATTLGHLECARVLLAHGADVGRENRSGWTVLQEAVSTRDLELVQLVLRY 95
Cdd:COG0666   145 DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA 208
 
Name Accession Description Interval E-value
GPCR_chapero_1 pfam11904
GPCR-chaperone; This domain, and the associated ANK family repeat pfam00023 domain, together ...
 155-493 4.91e-137

GPCR-chaperone; This domain, and the associated ANK family repeat pfam00023 domain, together act as a chaperone for biogenesis and folding of the DP receptor for prostaglandin D2.


Pssm-ID: 463391  Cd Length: 298  Bit Score: 402.01  E-value: 4.91e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462553036 155 RVDTTLLGFDHMTWQRGNRSFVFRGQDTS-AVVMEIDHDRRVVYTETLALAGQDRElllaaaqpTEEQVLSRLTAPVVTT 233
Cdd:pfam11904   1 RADTTLLGFDGFKWQRGDQSFLFLGDGDSpGSLLELDHDEKEVQLEGAGAEASEEE--------VEEEVAARLQTPIVRP 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462553036 234 QLDTKNISFERNKTGilgW-RSEKTEMVNGYEAKVYGASNVELITRTRTEHLSEQHKGKVK-------GCKTPLQSFLGI 305
Cdd:pfam11904  73 GIDVTKISFERNKSG---WrRQEKTEMVGGYKAKVYDASNVELSTKSRTEHLSEEEKAKLKsaleppeGSRTPLQSFLGI 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462553036 306 AEQHGGPQNGTLITQTLSQANPTAITAEEYFNPnfelgnrdmgrPMELTTKTQnvpyplgsgggRFKAKLWLCEEHPLSL 385
Cdd:pfam11904 150 AEEEKGWFGKTREESEAPPTNPTALTPEEYFDP-----------PKEESEKKK-----------GFKATLWLSEDFPLSL 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462553036 386 cEQVAPIIDLMAVSNALFAKLRDFITLRLPPGFPVKIEIPIFHILNARITFGNLNGCDePVPSVRGSPSSETPSPGsdss 465
Cdd:pfam11904 208 -EQLLPILDLLANKVKHFRRLREFITLKLPPGFPVKIEIPVFPTVNARITFTKFEELD-PVEEFSTPIKSPERGSP---- 281

                         330       340
                  ....*....|....*....|....*...
gi 2462553036 466 svsssssttscRGCEISPALFEAPRGYS 493
Cdd:pfam11904 282 -----------SSCEIDDDPFEIPSGYT 298
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
32-95 1.08e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 71.91  E-value: 1.08e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462553036  32 DIEQLDPRGRTPLHLATTLGHLECARVLLAHGADVGRENRSGWTVLQEAVSTRDLELVQLVLRY 95
Cdd:COG0666   145 DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA 208
Ank_2 pfam12796
Ankyrin repeats (3 copies);
31-93 5.55e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 59.36  E-value: 5.55e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462553036  31 VDIEQLDPRGRTPLHLATTLGHLECARVLLAHGAdvGRENRSGWTVLQEAVSTRDLELVQLVL 93
Cdd:pfam12796  21 ADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVKLLL 81
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 32-95 1.75e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.60  E-value: 1.75e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462553036  32 DIEQLDPRGRTPLHLATTLGHLECARVLLAHGADVGRENRSGWTVLQEAVSTRDLELVQLVLRY 95
Cdd:PTZ00322  107 DPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 39-66 5.66e-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: 40.26  E-value: 5.66e-05
                           10        20
                   ....*....|....*....|....*...
gi 2462553036   39 RGRTPLHLATTLGHLECARVLLAHGADV 66
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
 
Name Accession Description Interval E-value
GPCR_chapero_1 pfam11904
GPCR-chaperone; This domain, and the associated ANK family repeat pfam00023 domain, together ...
 155-493 4.91e-137

GPCR-chaperone; This domain, and the associated ANK family repeat pfam00023 domain, together act as a chaperone for biogenesis and folding of the DP receptor for prostaglandin D2.


Pssm-ID: 463391  Cd Length: 298  Bit Score: 402.01  E-value: 4.91e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462553036 155 RVDTTLLGFDHMTWQRGNRSFVFRGQDTS-AVVMEIDHDRRVVYTETLALAGQDRElllaaaqpTEEQVLSRLTAPVVTT 233
Cdd:pfam11904   1 RADTTLLGFDGFKWQRGDQSFLFLGDGDSpGSLLELDHDEKEVQLEGAGAEASEEE--------VEEEVAARLQTPIVRP 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462553036 234 QLDTKNISFERNKTGilgW-RSEKTEMVNGYEAKVYGASNVELITRTRTEHLSEQHKGKVK-------GCKTPLQSFLGI 305
Cdd:pfam11904  73 GIDVTKISFERNKSG---WrRQEKTEMVGGYKAKVYDASNVELSTKSRTEHLSEEEKAKLKsaleppeGSRTPLQSFLGI 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462553036 306 AEQHGGPQNGTLITQTLSQANPTAITAEEYFNPnfelgnrdmgrPMELTTKTQnvpyplgsgggRFKAKLWLCEEHPLSL 385
Cdd:pfam11904 150 AEEEKGWFGKTREESEAPPTNPTALTPEEYFDP-----------PKEESEKKK-----------GFKATLWLSEDFPLSL 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462553036 386 cEQVAPIIDLMAVSNALFAKLRDFITLRLPPGFPVKIEIPIFHILNARITFGNLNGCDePVPSVRGSPSSETPSPGsdss 465
Cdd:pfam11904 208 -EQLLPILDLLANKVKHFRRLREFITLKLPPGFPVKIEIPVFPTVNARITFTKFEELD-PVEEFSTPIKSPERGSP---- 281

                         330       340
                  ....*....|....*....|....*...
gi 2462553036 466 svsssssttscRGCEISPALFEAPRGYS 493
Cdd:pfam11904 282 -----------SSCEIDDDPFEIPSGYT 298
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
32-95 1.08e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 71.91  E-value: 1.08e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462553036  32 DIEQLDPRGRTPLHLATTLGHLECARVLLAHGADVGRENRSGWTVLQEAVSTRDLELVQLVLRY 95
Cdd:COG0666   145 DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA 208
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
31-95 2.79e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 70.75  E-value: 2.79e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462553036  31 VDIEQLDPRGRTPLHLATTLGHLECARVLLAHGADVGRENRSGWTVLQEAVSTRDLELVQLVLRY 95
Cdd:COG0666   111 ADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA 175
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
32-96 3.27e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 67.67  E-value: 3.27e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462553036  32 DIEQLDPRGRTPLHLATTLGHLECARVLLAHGADVGRENRSGWTVLQEAVSTRDLELVQLVLRYR 96
Cdd:COG0666   178 DVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242
Ank_2 pfam12796
Ankyrin repeats (3 copies);
31-93 5.55e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 59.36  E-value: 5.55e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462553036  31 VDIEQLDPRGRTPLHLATTLGHLECARVLLAHGAdvGRENRSGWTVLQEAVSTRDLELVQLVL 93
Cdd:pfam12796  21 ADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVKLLL 81
Ank_4 pfam13637
Ankyrin repeats (many copies);
40-93 5.37e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.36  E-value: 5.37e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462553036  40 GRTPLHLATTLGHLECARVLLAHGADVGRENRSGWTVLQEAVSTRDLELVQLVL 93
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
31-95 1.53e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 59.58  E-value: 1.53e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462553036  31 VDIEQLDPRGRTPLHLATTLGHLECARVLLAHGADVGRENRSGWTVLQEAVSTRDLELVQLVLRY 95
Cdd:COG0666    78 ADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA 142
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 32-95 1.75e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.60  E-value: 1.75e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462553036  32 DIEQLDPRGRTPLHLATTLGHLECARVLLAHGADVGRENRSGWTVLQEAVSTRDLELVQLVLRY 95
Cdd:PTZ00322  107 DPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
Ank_2 pfam12796
Ankyrin repeats (3 copies);
44-97 6.67e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 50.50  E-value: 6.67e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462553036  44 LHLATTLGHLECARVLLAHGADVGRENRSGWTVLQEAVSTRDLELVQLVLRYRD 97
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
30-80 1.20e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.50  E-value: 1.20e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462553036  30 QVDIEQLDPRGRTPLHLATTLGHLECARVLLAHGADVGRENRSGWTVLQEA 80
Cdd:pfam13857   6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_2 pfam12796
Ankyrin repeats (3 copies);
36-70 9.87e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 47.03  E-value: 9.87e-07
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2462553036  36 LDPRGRTPLHLATTLGHLECARVLLAHGADVGREN 70
Cdd:pfam12796  57 LKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 39-71 2.31e-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: 2.31e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2462553036  39 RGRTPLHLA-TTLGHLECARVLLAHGADVGRENR 71
Cdd:pfam00023   1 DGNTPLHLAaGRRGNLEIVKLLLSKGADVNARDK 34
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 39-96 6.10e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 48.83  E-value: 6.10e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462553036  39 RGRTPLHLATTLGHLECARVLLAHGADVGRENRSGWTVLQEAVSTRDLELVQLVLRYR 96
Cdd:PHA02875  101 DGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHK 158
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 37-84 1.06e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 48.71  E-value: 1.06e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2462553036  37 DPRGRTPLHLATTLGHLECARVLLAHGADVGRENRSGWTVLQEAVSTR 84
Cdd:PLN03192  555 DSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAK 602
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 39-66 5.66e-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: 40.26  E-value: 5.66e-05
                           10        20
                   ....*....|....*....|....*...
gi 2462553036   39 RGRTPLHLATTLGHLECARVLLAHGADV 66
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
32-96 3.00e-04

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 43.02  E-value: 3.00e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462553036  32 DIEQLDPRGRTPLHLATTLGHLECARVLLAHGADVGRENRSGWTVLQEAVSTRDLELVQLVLRYR 96
Cdd:COG0666   211 DVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLAL 275
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 39-66 3.25e-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: 38.39  E-value: 3.25e-04
                          10        20
                  ....*....|....*....|....*...
gi 2462553036  39 RGRTPLHLATTLGHLECARVLLAHGADV 66
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 31-96 1.38e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 41.59  E-value: 1.38e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462553036  31 VDIEQLDPRGRTPLHLATTLGHLECARVLLAHGADVGRENRSGWTVLQEAVSTRDLELVQLVLRYR 96
Cdd:PHA02876  169 ADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNR 234
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 31-97 1.88e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 41.19  E-value: 1.88e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462553036  31 VDIEQLDPRGRTPLHLATTLGHLECARVLLAHGADVGRENRSGWTVLQEAVSTRDLELVQLVLRYRD 97
Cdd:PHA03100  183 VPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249
PHA02795 PHA02795
ankyrin-like protein; Provisional
 32-94 6.23e-03

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 39.59  E-value: 6.23e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462553036  32 DIEQLDPRGRTPLHLATTLGHLECARVLLAHGADVGRENRSGWTVLQEAV------STRD--LELVQLVLR 94
Cdd:PHA02795  213 DINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVdrgsviARREthLKILEILLR 283
 
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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