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Conserved domains on  [gi|269315852|ref|NP_997237|]
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ankyrin repeat domain-containing protein 13D isoform 1 [Homo sapiens]

Protein Classification

ankyrin repeat domain-containing protein 13( domain architecture ID 12122236)

ankyrin repeat domain-containing protein 13 is involved in regulating the internalization of ubiquitinated epidermal growth factor receptor (EGFR) from the cell surface

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 ...
 155-469 2.17e-141

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: 412.03  E-value: 2.17e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269315852  155 RVDTSLLGFEHMTWQRGRRSFIFKGQ-EAGALVMEVDHDRQVVHVETLGLTLQEPEtllaamrpSEEHVASRLTSPIVST 233
Cdd:pfam11904   1 RADTTLLGFDGFKWQRGDQSFLFLGDgDSPGSLLELDHDEKEVQLEGAGAEASEEE--------VEEEVAARLQTPIVRP 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269315852  234 HLDTRNVAFERNKCGiWGwRSEKMETVSGYEAKVYSATNVELVTRTRTEHLSDQDKSRSKA-------GKTPFQSFLGMA 306
Cdd:pfam11904  73 GIDVTKISFERNKSG-WR-RQEKTEMVGGYKAKVYDASNVELSTKSRTEHLSEEEKAKLKSaleppegSRTPLQSFLGIA 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269315852  307 QQHSSH-TGAPVQQAASPTNPTAISPEEYFDPnfslesrnigrPIEMSSKVQRFKATLWLSEEHPLSLgDQVTPIIDLMA 385
Cdd:pfam11904 151 EEEKGWfGKTREESEAPPTNPTALTPEEYFDP-----------PKEESEKKKGFKATLWLSEDFPLSL-EQLLPILDLLA 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269315852  386 ISNAHFAKLRDFITLRLPPGFPVKIEIPLFHVLNARITFSNLCGCDePLSSVWVPAPSSavaASGNPFPCEVDPTVFEVP 465
Cdd:pfam11904 219 NKVKHFRRLREFITLKLPPGFPVKIEIPVFPTVNARITFTKFEELD-PVEEFSTPIKSP---ERGSPSSCEIDDDPFEIP 294


                  ....
gi 269315852  466 NGYS 469
Cdd:pfam11904 295 SGYT 298
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
9-95 7.15e-13

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 69.60  E-value: 7.15e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269315852   9 PLHRLVWANrHRELEAALHSHQHDIEQEDPRGRTPLELAVSLGNLESVRVLLRHNANVGKENRQGWAVLQEAVSTGDPEM 88
Cdd:COG0666   90 LLHAAARNG-DLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEI 168


                 ....*..
gi 269315852  89 VQLVLQY 95
Cdd:COG0666  169 VKLLLEA 175
 
Name Accession Description Interval E-value
GPCR_chapero_1 pfam11904
GPCR-chaperone; This domain, and the associated ANK family repeat pfam00023 domain, together ...
 155-469 2.17e-141

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: 412.03  E-value: 2.17e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269315852  155 RVDTSLLGFEHMTWQRGRRSFIFKGQ-EAGALVMEVDHDRQVVHVETLGLTLQEPEtllaamrpSEEHVASRLTSPIVST 233
Cdd:pfam11904   1 RADTTLLGFDGFKWQRGDQSFLFLGDgDSPGSLLELDHDEKEVQLEGAGAEASEEE--------VEEEVAARLQTPIVRP 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269315852  234 HLDTRNVAFERNKCGiWGwRSEKMETVSGYEAKVYSATNVELVTRTRTEHLSDQDKSRSKA-------GKTPFQSFLGMA 306
Cdd:pfam11904  73 GIDVTKISFERNKSG-WR-RQEKTEMVGGYKAKVYDASNVELSTKSRTEHLSEEEKAKLKSaleppegSRTPLQSFLGIA 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269315852  307 QQHSSH-TGAPVQQAASPTNPTAISPEEYFDPnfslesrnigrPIEMSSKVQRFKATLWLSEEHPLSLgDQVTPIIDLMA 385
Cdd:pfam11904 151 EEEKGWfGKTREESEAPPTNPTALTPEEYFDP-----------PKEESEKKKGFKATLWLSEDFPLSL-EQLLPILDLLA 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269315852  386 ISNAHFAKLRDFITLRLPPGFPVKIEIPLFHVLNARITFSNLCGCDePLSSVWVPAPSSavaASGNPFPCEVDPTVFEVP 465
Cdd:pfam11904 219 NKVKHFRRLREFITLKLPPGFPVKIEIPVFPTVNARITFTKFEELD-PVEEFSTPIKSP---ERGSPSSCEIDDDPFEIP 294


                  ....
gi 269315852  466 NGYS 469
Cdd:pfam11904 295 SGYT 298
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
9-95 7.15e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 69.60  E-value: 7.15e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269315852   9 PLHRLVWANrHRELEAALHSHQHDIEQEDPRGRTPLELAVSLGNLESVRVLLRHNANVGKENRQGWAVLQEAVSTGDPEM 88
Cdd:COG0666   90 LLHAAARNG-DLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEI 168


                 ....*..
gi 269315852  89 VQLVLQY 95
Cdd:COG0666  169 VKLLLEA 175
Ank_2 pfam12796
Ankyrin repeats (3 copies);
13-95 5.98e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 53.58  E-value: 5.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269315852   13 LVWANRHRELEAA--LHSHQHDIEQEDPRGRTPLELAVSLGNLESVRVLLRHNAnvGKENRQGWAVLQEAVSTGDPEMVQ 90
Cdd:pfam12796   1 LHLAAKNGNLELVklLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78


                  ....*
gi 269315852   91 LVLQY 95
Cdd:pfam12796  79 LLLEK 83
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 37-95 9.39e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 45.63  E-value: 9.39e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 269315852  37 DPRGRTPLELAVSLGNLESVRVLLRHNANVGKENRQGWAVLQEAVSTGDPEMVQLVLQY 95
Cdd:PLN03192 555 DSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHF 613
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 39-66 1.75e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.03  E-value: 1.75e-03
                           10        20
                   ....*....|....*....|....*...
gi 269315852    39 RGRTPLELAVSLGNLESVRVLLRHNANV 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 ...
 155-469 2.17e-141

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: 412.03  E-value: 2.17e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269315852  155 RVDTSLLGFEHMTWQRGRRSFIFKGQ-EAGALVMEVDHDRQVVHVETLGLTLQEPEtllaamrpSEEHVASRLTSPIVST 233
Cdd:pfam11904   1 RADTTLLGFDGFKWQRGDQSFLFLGDgDSPGSLLELDHDEKEVQLEGAGAEASEEE--------VEEEVAARLQTPIVRP 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269315852  234 HLDTRNVAFERNKCGiWGwRSEKMETVSGYEAKVYSATNVELVTRTRTEHLSDQDKSRSKA-------GKTPFQSFLGMA 306
Cdd:pfam11904  73 GIDVTKISFERNKSG-WR-RQEKTEMVGGYKAKVYDASNVELSTKSRTEHLSEEEKAKLKSaleppegSRTPLQSFLGIA 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269315852  307 QQHSSH-TGAPVQQAASPTNPTAISPEEYFDPnfslesrnigrPIEMSSKVQRFKATLWLSEEHPLSLgDQVTPIIDLMA 385
Cdd:pfam11904 151 EEEKGWfGKTREESEAPPTNPTALTPEEYFDP-----------PKEESEKKKGFKATLWLSEDFPLSL-EQLLPILDLLA 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269315852  386 ISNAHFAKLRDFITLRLPPGFPVKIEIPLFHVLNARITFSNLCGCDePLSSVWVPAPSSavaASGNPFPCEVDPTVFEVP 465
Cdd:pfam11904 219 NKVKHFRRLREFITLKLPPGFPVKIEIPVFPTVNARITFTKFEELD-PVEEFSTPIKSP---ERGSPSSCEIDDDPFEIP 294


                  ....
gi 269315852  466 NGYS 469
Cdd:pfam11904 295 SGYT 298
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
9-95 7.15e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 69.60  E-value: 7.15e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269315852   9 PLHRLVWANrHRELEAALHSHQHDIEQEDPRGRTPLELAVSLGNLESVRVLLRHNANVGKENRQGWAVLQEAVSTGDPEM 88
Cdd:COG0666   90 LLHAAARNG-DLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEI 168


                 ....*..
gi 269315852  89 VQLVLQY 95
Cdd:COG0666  169 VKLLLEA 175
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
9-95 4.39e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 67.29  E-value: 4.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269315852   9 PLHRLVWANrHRELEAALHSHQHDIEQEDPRGRTPLELAVSLGNLESVRVLLRHNANVGKENRQGWAVLQEAVSTGDPEM 88
Cdd:COG0666  123 PLHLAAYNG-NLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEI 201


                 ....*..
gi 269315852  89 VQLVLQY 95
Cdd:COG0666  202 VKLLLEA 208
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
9-126 3.36e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 61.51  E-value: 3.36e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269315852   9 PLHRLVWANrHRELEAALHSHQHDIEQEDPRGRTPLELAVSLGNLESVRVLLRHNANVGKENRQGWAVLQEAVSTGDPEM 88
Cdd:COG0666  156 PLHLAAANG-NLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI 234

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 269315852  89 VQLVLQYRDYQRATQRLAGIPELLNKLRQAPDFYVEMK 126
Cdd:COG0666  235 VKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLL 272
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
9-95 9.50e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 59.97  E-value: 9.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269315852   9 PLHRLVWANRHRELEAALHSHQHDIEQEDPRGRTPLELAVSLGNLESVRVLLRHNANVGKENRQGWAVLQEAVSTGDPEM 88
Cdd:COG0666   56 LLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI 135


                 ....*..
gi 269315852  89 VQLVLQY 95
Cdd:COG0666  136 VKLLLEA 142
Ank_2 pfam12796
Ankyrin repeats (3 copies);
13-95 5.98e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 53.58  E-value: 5.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269315852   13 LVWANRHRELEAA--LHSHQHDIEQEDPRGRTPLELAVSLGNLESVRVLLRHNAnvGKENRQGWAVLQEAVSTGDPEMVQ 90
Cdd:pfam12796   1 LHLAAKNGNLELVklLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78


                  ....*
gi 269315852   91 LVLQY 95
Cdd:pfam12796  79 LLLEK 83
Ank_4 pfam13637
Ankyrin repeats (many copies);
40-93 1.97e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.04  E-value: 1.97e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 269315852   40 GRTPLELAVSLGNLESVRVLLRHNANVGKENRQGWAVLQEAVSTGDPEMVQLVL 93
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
44-97 1.40e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 46.65  E-value: 1.40e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 269315852   44 LELAVSLGNLESVRVLLRHNANVGKENRQGWAVLQEAVSTGDPEMVQLVLQYRD 97
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
26-80 6.65e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.79  E-value: 6.65e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 269315852   26 LHSHQH-DIEQEDPRGRTPLELAVSLGNLESVRVLLRHNANVGKENRQGWAVLQEA 80
Cdd:pfam13857   1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 37-95 9.39e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 45.63  E-value: 9.39e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 269315852  37 DPRGRTPLELAVSLGNLESVRVLLRHNANVGKENRQGWAVLQEAVSTGDPEMVQLVLQY 95
Cdd:PLN03192 555 DSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHF 613
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 4-96 1.02e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 44.98  E-value: 1.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269315852   4 PGPTFPLHRLVWANRHRELEAALHSHQHDIEQEDPRGRTPLELAVSLGNLESVRVLLRHNANVGKENRQGWAVLQEAVST 83
Cdd:PHA02875  66 PDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMM 145

                         90
                 ....*....|...
gi 269315852  84 GDPEMVQLVLQYR 96
Cdd:PHA02875 146 GDIKGIELLIDHK 158
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 32-121 1.90e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.50  E-value: 1.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269315852  32 DIEQEDPRGRTPLELAVSLGNLESVRVLLRHNANVGKENRQGWAVLQEAVSTGDPEMVQLVLQYR------DYQRATQRL 105
Cdd:PTZ00322 107 DPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSqchfelGANAKPDSF 186

                         90
                 ....*....|....*....
gi 269315852 106 AGIPELLNK---LRQAPDF 121
Cdd:PTZ00322 187 TGKPPSLEDspiSSHHPDF 205
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 7-94 7.32e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 42.29  E-value: 7.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269315852   7 TFPLHRLVWANRHRELEAALhSHQHDIEQEDPRGRTPLELAVSLGNLESVRVLLRHNANVGKENRQG-WAVLQEAVSTGD 85
Cdd:PHA02875 136 FSPLHLAVMMGDIKGIELLI-DHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNK 214


                 ....*....
gi 269315852  86 PEMVQLVLQ 94
Cdd:PHA02875 215 IDIVRLFIK 223
Ank_2 pfam12796
Ankyrin repeats (3 copies);
30-70 1.21e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 38.17  E-value: 1.21e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 269315852   30 QHDIEQEDPRGRTPLELAVSLGNLESVRVLLRHNANVGKEN 70
Cdd:pfam12796  51 EHADVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 39-66 1.68e-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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.08  E-value: 1.68e-03
                          10        20
                  ....*....|....*....|....*...
gi 269315852   39 RGRTPLELAVSLGNLESVRVLLRHNANV 66
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 39-66 1.75e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.03  E-value: 1.75e-03
                           10        20
                   ....*....|....*....|....*...
gi 269315852    39 RGRTPLELAVSLGNLESVRVLLRHNANV 66
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 39-71 1.80e-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: 36.11  E-value: 1.80e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 269315852   39 RGRTPLELAV-SLGNLESVRVLLRHNANVGKENR 71
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
 
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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