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Conserved domains on  [gi|2217331089|ref|XP_047301807|]
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CAP-Gly domain-containing linker protein 4 isoform X5 [Homo sapiens]

Protein Classification

CAP-Gly domain-containing linker protein; CAP-Gly domain-containing protein( domain architecture ID 12790878)

CAP-Gly domain-containing linker protein functions as a cytoplasmic linker protein; CAP-Gly domain-containing protein similar to human dynactin-1 and Saccharomyces cerevisiae nuclear fusion protein BIK1; CAP-Gly domains serve as recognition domains for EEY/F-COO(-) motifs

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 285-349 1.71e-32

CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of microtubules and transportation of vesicles and organelles along the cytoskeletal network. A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.


:

Pssm-ID: 460154 [Multi-domain]  Cd Length: 65  Bit Score: 118.27  E-value: 1.71e-32
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217331089 285 LGDRVVIAGQKVGTLRFCGTTEFASGQWAGIELDEPEGKNNGSVGKVQYFKCAPKYGIFAPLSKI 349
Cdd:pfam01302   1 VGDRVEVPGGRRGTVRYVGPVPFAPGVWVGVELDEPVGKNDGSVKGVRYFECPPKHGVFVRPSKV 65
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
84-225 1.81e-18

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 85.78  E-value: 1.81e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217331089  84 NIDIIgNEILKRGCNVNDRDGLtDMTLLHYtcksgAHGIGDVEtAVKFatqLIDLGADISLRSRWtNMNALHYAAYFDVP 163
Cdd:COG0666    99 DLEIV-KLLLEAGADVNARDKD-GETPLHL-----AAYNGNLE-IVKL---LLEAGADVNAQDND-GNTPLHLAAANGNL 166

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217331089 164 ELIRVILKtsKPKDVDATcsDFNFGTALHIAAYNLCAGAVKCLLEQGANPAFRNDKGQIPAD 225
Cdd:COG0666   167 EIVKLLLE--AGADVNAR--DNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALD 224
 
Name Accession Description Interval E-value
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 285-349 1.71e-32

CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of microtubules and transportation of vesicles and organelles along the cytoskeletal network. A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.


Pssm-ID: 460154 [Multi-domain]  Cd Length: 65  Bit Score: 118.27  E-value: 1.71e-32
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217331089 285 LGDRVVIAGQKVGTLRFCGTTEFASGQWAGIELDEPEGKNNGSVGKVQYFKCAPKYGIFAPLSKI 349
Cdd:pfam01302   1 VGDRVEVPGGRRGTVRYVGPVPFAPGVWVGVELDEPVGKNDGSVKGVRYFECPPKHGVFVRPSKV 65
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
 285-350 1.43e-28

Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and transportation of vesicles and organelles along the cytoskeletal network; A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.


Pssm-ID: 214997 [Multi-domain]  Cd Length: 68  Bit Score: 107.67  E-value: 1.43e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217331089  285 LGDRV-VIAGQKVGTLRFCGTTEFASGQWAGIELDEPE-GKNNGSVGKVQYFKCAPKYGIFAPLSKIS 350
Cdd:smart01052   1 VGDRVeVGGGGRRGTVRYVGPTPFAPGVWVGVELDEPLrGKNDGSVKGVRYFECPPKHGIFVRPSKVE 68
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
84-225 1.81e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 85.78  E-value: 1.81e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217331089  84 NIDIIgNEILKRGCNVNDRDGLtDMTLLHYtcksgAHGIGDVEtAVKFatqLIDLGADISLRSRWtNMNALHYAAYFDVP 163
Cdd:COG0666    99 DLEIV-KLLLEAGADVNARDKD-GETPLHL-----AAYNGNLE-IVKL---LLEAGADVNAQDND-GNTPLHLAAANGNL 166

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217331089 164 ELIRVILKtsKPKDVDATcsDFNFGTALHIAAYNLCAGAVKCLLEQGANPAFRNDKGQIPAD 225
Cdd:COG0666   167 EIVKLLLE--AGADVNAR--DNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALD 224
NIP100 COG5244
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ...
 283-343 2.24e-15

Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 227569 [Multi-domain]  Cd Length: 669  Bit Score: 78.96  E-value: 2.24e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217331089 283 LKLGDRVVIaGQKVGTLRFCGTTEFASGQWAGIELDEPEGKNNGSVGKVQYFKCAPKYGIF 343
Cdd:COG5244     4 LSVNDRVLL-GDKFGTVRFIGKTKFKDGIWIGLELDDPVGKNDGSVNGVRYFHCKKRHGIF 63
Ank_2 pfam12796
Ankyrin repeats (3 copies);
111-217 9.82e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 55.51  E-value: 9.82e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217331089 111 LHYTCKSGAHGIgdvetaVKFatqLIDLGADISLRSRWtNMNALHYAAYFDVPELIRVILKTskpKDVDATCSDFnfgTA 190
Cdd:pfam12796   1 LHLAAKNGNLEL------VKL---LLENGADANLQDKN-GRTALHLAAKNGHLEIVKLLLEH---ADVNLKDNGR---TA 64

                          90       100
                  ....*....|....*....|....*..
gi 2217331089 191 LHIAAYNLCAGAVKCLLEQGANPAFRN 217
Cdd:pfam12796  65 LHYAARSGHLEIVKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 92-226 1.29e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 53.88  E-value: 1.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217331089  92 ILKRGCNVNDRDGLtDMTLLHYTCKSGahgIGDVETAVKFatqLIDLGADISLRSRwTNMNALHYAAYFD-VPELIRVIL 170
Cdd:PHA03095   33 LLAAGADVNFRGEY-GKTPLHLYLHYS---SEKVKDIVRL---LLEAGADVNAPER-CGFTPLHLYLYNAtTLDVIKLLI 104

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2217331089 171 KtskpKDVDATCSDFNFGTALHIAAYNLC--AGAVKCLLEQGANPAFRNDKGQIPADV 226
Cdd:PHA03095  105 K----AGADVNAKDKVGRTPLHVYLSGFNinPKVIRLLLRKGADVNALDLYGMTPLAV 158
 
Name Accession Description Interval E-value
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 285-349 1.71e-32

CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of microtubules and transportation of vesicles and organelles along the cytoskeletal network. A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.


Pssm-ID: 460154 [Multi-domain]  Cd Length: 65  Bit Score: 118.27  E-value: 1.71e-32
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217331089 285 LGDRVVIAGQKVGTLRFCGTTEFASGQWAGIELDEPEGKNNGSVGKVQYFKCAPKYGIFAPLSKI 349
Cdd:pfam01302   1 VGDRVEVPGGRRGTVRYVGPVPFAPGVWVGVELDEPVGKNDGSVKGVRYFECPPKHGVFVRPSKV 65
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
 285-350 1.43e-28

Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and transportation of vesicles and organelles along the cytoskeletal network; A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.


Pssm-ID: 214997 [Multi-domain]  Cd Length: 68  Bit Score: 107.67  E-value: 1.43e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217331089  285 LGDRV-VIAGQKVGTLRFCGTTEFASGQWAGIELDEPE-GKNNGSVGKVQYFKCAPKYGIFAPLSKIS 350
Cdd:smart01052   1 VGDRVeVGGGGRRGTVRYVGPTPFAPGVWVGVELDEPLrGKNDGSVKGVRYFECPPKHGIFVRPSKVE 68
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
84-225 1.81e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 85.78  E-value: 1.81e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217331089  84 NIDIIgNEILKRGCNVNDRDGLtDMTLLHYtcksgAHGIGDVEtAVKFatqLIDLGADISLRSRWtNMNALHYAAYFDVP 163
Cdd:COG0666    99 DLEIV-KLLLEAGADVNARDKD-GETPLHL-----AAYNGNLE-IVKL---LLEAGADVNAQDND-GNTPLHLAAANGNL 166

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217331089 164 ELIRVILKtsKPKDVDATcsDFNFGTALHIAAYNLCAGAVKCLLEQGANPAFRNDKGQIPAD 225
Cdd:COG0666   167 EIVKLLLE--AGADVNAR--DNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALD 224
NIP100 COG5244
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ...
 283-343 2.24e-15

Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 227569 [Multi-domain]  Cd Length: 669  Bit Score: 78.96  E-value: 2.24e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217331089 283 LKLGDRVVIaGQKVGTLRFCGTTEFASGQWAGIELDEPEGKNNGSVGKVQYFKCAPKYGIF 343
Cdd:COG5244     4 LSVNDRVLL-GDKFGTVRFIGKTKFKDGIWIGLELDDPVGKNDGSVNGVRYFHCKKRHGIF 63
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
84-225 8.71e-14

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 71.91  E-value: 8.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217331089  84 NIDIIgNEILKRGCNVNDRDGlTDMTLLHYTCKSGahgigDVEtAVKFatqLIDLGADISLRSRwTNMNALHYAAYFDVP 163
Cdd:COG0666   132 NLEIV-KLLLEAGADVNAQDN-DGNTPLHLAAANG-----NLE-IVKL---LLEAGADVNARDN-DGETPLHLAAENGHL 199

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217331089 164 ELIRVILKtsKPKDVDATcsDFNFGTALHIAAYNLCAGAVKCLLEQGANPAFRNDKGQIPAD 225
Cdd:COG0666   200 EIVKLLLE--AGADVNAK--DNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALL 257
Ank_2 pfam12796
Ankyrin repeats (3 copies);
111-217 9.82e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 55.51  E-value: 9.82e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217331089 111 LHYTCKSGAHGIgdvetaVKFatqLIDLGADISLRSRWtNMNALHYAAYFDVPELIRVILKTskpKDVDATCSDFnfgTA 190
Cdd:pfam12796   1 LHLAAKNGNLEL------VKL---LLENGADANLQDKN-GRTALHLAAKNGHLEIVKLLLEH---ADVNLKDNGR---TA 64

                          90       100
                  ....*....|....*....|....*..
gi 2217331089 191 LHIAAYNLCAGAVKCLLEQGANPAFRN 217
Cdd:pfam12796  65 LHYAARSGHLEIVKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 92-226 1.29e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 53.88  E-value: 1.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217331089  92 ILKRGCNVNDRDGLtDMTLLHYTCKSGahgIGDVETAVKFatqLIDLGADISLRSRwTNMNALHYAAYFD-VPELIRVIL 170
Cdd:PHA03095   33 LLAAGADVNFRGEY-GKTPLHLYLHYS---SEKVKDIVRL---LLEAGADVNAPER-CGFTPLHLYLYNAtTLDVIKLLI 104

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2217331089 171 KtskpKDVDATCSDFNFGTALHIAAYNLC--AGAVKCLLEQGANPAFRNDKGQIPADV 226
Cdd:PHA03095  105 K----AGADVNAKDKVGRTPLHVYLSGFNinPKVIRLLLRKGADVNALDLYGMTPLAV 158
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
84-220 2.41e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 52.26  E-value: 2.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217331089  84 NIDIIgNEILKRGCNVNDRDGLtDMTLLHYTCKSGAHGIgdvetaVKFatqLIDLGADISLRSRWtNMNALHYAAYFDVP 163
Cdd:COG0666   165 NLEIV-KLLLEAGADVNARDND-GETPLHLAAENGHLEI------VKL---LLEAGADVNAKDND-GKTALDLAAENGNL 232

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2217331089 164 ELIRVILKTSKPKDVDatcsDFNFGTALHIAAYNLCAGAVKCLLEQGANPAFRNDKG 220
Cdd:COG0666   233 EIVKLLLEAGADLNAK----DKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285
Ank_4 pfam13637
Ankyrin repeats (many copies);
150-207 4.04e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.11  E-value: 4.04e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2217331089 150 NMNALHYAAYFDVPELIRVILKtsKPKDVDATCSDFNfgTALHIAAYNLCAGAVKCLL 207
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLE--KGADINAVDGNGE--TALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 92-256 1.18e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 44.27  E-value: 1.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217331089  92 ILKRGCNVNDRDGLTDMTLLHYTCKSGAHgigdvETAVKFatqLIDLGADISLrSRWTNMNALHYAAYFDVPELirVILK 171
Cdd:PHA03100   92 LLEYGANVNAPDNNGITPLLYAISKKSNS-----YSIVEY---LLDNGANVNI-KNSDGENLLHLYLESNKIDL--KILK 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217331089 172 T--SKPKDVDATCS--------------DFNFGTALHIAAYNLCAGAVKCLLEQGANPAFRNDKGqipadvvpdpvDMPL 235
Cdd:PHA03100  161 LliDKGVDINAKNRvnyllsygvpinikDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYG-----------DTPL 229

                         170       180
                  ....*....|....*....|.
gi 2217331089 236 EMAdAAATAKEIKQMLLDAVP 256
Cdd:PHA03100  230 HIA-ILNNNKEIFKLLLNNGP 249
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
128-254 9.99e-04

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 41.09  E-value: 9.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217331089 128 AVKFATQLIDLGADISLRSRWTNMNALHYAAYFDVPELIRVILKTskpKDVDATCSDFNFGTALHIAAYNLCAGAVKCLL 207
Cdd:COG0666    31 LLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLA---AGADINAKDDGGNTLLHAAARNGDLEIVKLLL 107

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2217331089 208 EQGANPAFRNDKGQIpadvvpdpvdmPLEMAdAAATAKEIKQMLLDA 254
Cdd:COG0666   108 EAGADVNARDKDGET-----------PLHLA-AYNGNLEIVKLLLEA 142
PHA03095 PHA03095
ankyrin-like protein; Provisional
 84-224 7.26e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 38.85  E-value: 7.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217331089  84 NIDIIgNEILKRGCNVNDRDgLTDMTLLHYTCKSgahgigdVETAVKFATQLIDLGADISLRSRWTNmNALHYAAYFDVP 163
Cdd:PHA03095  166 NVELL-RLLIDAGADVYAVD-DRFRSLLHHHLQS-------FKPRARIVRELIRAGCDPAATDMLGN-TPLHSMATGSSC 235

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217331089 164 ELIRV---ILKTSkpkDVDATcsDFNFGTALHIAAYNLCAGAVKCLLEQGANPAFRNDKGQIPA 224
Cdd:PHA03095  236 KRSLVlplLIAGI---SINAR--NRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 189-218 8.62e-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: 34.19  E-value: 8.62e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2217331089 189 TALHIAAYNL-CAGAVKCLLEQGANPAFRND 218
Cdd:pfam00023   4 TPLHLAAGRRgNLEIVKLLLSKGADVNARDK 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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