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Conserved domains on  [gi|767915242|ref|XP_011531412|]
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CAP-Gly domain-containing linker protein 4 isoform X4 [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 ...
 380-444 1.82e-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: 119.04  E-value: 1.82e-32
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767915242  380 LGERVLVVGQRLGTIRFFGTTNFAPGYWYGIELEKPHGKNDGSVGGVQYFSCSPRYGIFAPPSRV 444
Cdd:pfam01302   1 VGDRVEVPGGRRGTVRYVGPVPFAPGVWVGVELDEPVGKNDGSVKGVRYFECPPKHGVFVRPSKV 65
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 178-242 1.46e-31

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: 116.35  E-value: 1.46e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767915242  178 LGDRVVIAGQKVGTLRFCGTTEFASGQWAGIELDEPEGKNNGSVGKVQYFKCAPKYGIFAPLSKI 242
Cdd:pfam01302   1 VGDRVEVPGGRRGTVRYVGPVPFAPGVWVGVELDEPVGKNDGSVKGVRYFECPPKHGVFVRPSKV 65
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 519-583 4.36e-29

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: 109.41  E-value: 4.36e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767915242  519 GSQVLlTSSNEMGTVRYVGPTDFASGIWLGLELRSAKGKNDGSVGDKRYFTCKPNHGVLVRPSRV 583
Cdd:pfam01302   2 GDRVE-VPGGRRGTVRYVGPVPFAPGVWVGVELDEPVGKNDGSVKGVRYFECPPKHGVFVRPSKV 65
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-118 6.61e-15

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 75.38  E-value: 6.61e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915242   1 MTLLHYtcksgAHGIGDVEtAVKFatqLIDLGADISLRSRWtNMNALHYAAYFDVPELIRVILKtsKPKDVDATcsDFNF 80
Cdd:COG0666  121 ETPLHL-----AAYNGNLE-IVKL---LLEAGADVNAQDND-GNTPLHLAAANGNLEIVKLLLE--AGADVNAR--DNDG 186

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 767915242  81 GTALHIAAYNLCAGAVKCLLEQGANPAFRNDKGQIPAD 118
Cdd:COG0666  187 ETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALD 224
 
Name Accession Description Interval E-value
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 380-444 1.82e-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: 119.04  E-value: 1.82e-32
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767915242  380 LGERVLVVGQRLGTIRFFGTTNFAPGYWYGIELEKPHGKNDGSVGGVQYFSCSPRYGIFAPPSRV 444
Cdd:pfam01302   1 VGDRVEVPGGRRGTVRYVGPVPFAPGVWVGVELDEPVGKNDGSVKGVRYFECPPKHGVFVRPSKV 65
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 178-242 1.46e-31

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: 116.35  E-value: 1.46e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767915242  178 LGDRVVIAGQKVGTLRFCGTTEFASGQWAGIELDEPEGKNNGSVGKVQYFKCAPKYGIFAPLSKI 242
Cdd:pfam01302   1 VGDRVEVPGGRRGTVRYVGPVPFAPGVWVGVELDEPVGKNDGSVKGVRYFECPPKHGVFVRPSKV 65
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 519-583 4.36e-29

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: 109.41  E-value: 4.36e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767915242  519 GSQVLlTSSNEMGTVRYVGPTDFASGIWLGLELRSAKGKNDGSVGDKRYFTCKPNHGVLVRPSRV 583
Cdd:pfam01302   2 GDRVE-VPGGRRGTVRYVGPVPFAPGVWVGVELDEPVGKNDGSVKGVRYFECPPKHGVFVRPSKV 65
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
 178-243 3.17e-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: 107.29  E-value: 3.17e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767915242   178 LGDRV-VIAGQKVGTLRFCGTTEFASGQWAGIELDEPE-GKNNGSVGKVQYFKCAPKYGIFAPLSKIS 243
Cdd:smart01052   1 VGDRVeVGGGGRRGTVRYVGPTPFAPGVWVGVELDEPLrGKNDGSVKGVRYFECPPKHGIFVRPSKVE 68
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
 380-445 4.05e-27

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: 104.20  E-value: 4.05e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767915242   380 LGERVLVVG-QRLGTIRFFGTTNFAPGYWYGIELEKPH-GKNDGSVGGVQYFSCSPRYGIFAPPSRVQ 445
Cdd:smart01052   1 VGDRVEVGGgGRRGTVRYVGPTPFAPGVWVGVELDEPLrGKNDGSVKGVRYFECPPKHGIFVRPSKVE 68
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
 519-584 7.82e-27

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: 103.43  E-value: 7.82e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767915242   519 GSQVLLTSSNEMGTVRYVGPTDFASGIWLGLELR-SAKGKNDGSVGDKRYFTCKPNHGVLVRPSRVT 584
Cdd:smart01052   2 GDRVEVGGGGRRGTVRYVGPTPFAPGVWVGVELDePLRGKNDGSVKGVRYFECPPKHGIFVRPSKVE 68
NIP100 COG5244
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ...
 378-507 6.00e-18

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: 87.82  E-value: 6.00e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915242 378 LRLGERVLVvGQRLGTIRFFGTTNFAPGYWYGIELEKPHGKNDGSVGGVQYFSCSPRYGIFAPP--SRVQRVTDSLDTLS 455
Cdd:COG5244    4 LSVNDRVLL-GDKFGTVRFIGKTKFKDGIWIGLELDDPVGKNDGSVNGVRYFHCKKRHGIFIRPddDSLLNGNAAYEKIK 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767915242 456 EISSNKQNhsypgfrrSFSTTSASSQKEINRRNAFSKSKAalrRSWSSTPTA 507
Cdd:COG5244   83 GGLVCESK--------GMDKDGEIKQENHEDRIHFEESKI---RRLEETIEA 123
NIP100 COG5244
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ...
 515-580 2.17e-17

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: 85.89  E-value: 2.17e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767915242 515 KLHEGSQVLLtsSNEMGTVRYVGPTDFASGIWLGLELRSAKGKNDGSVGDKRYFTCKPNHGVLVRP 580
Cdd:COG5244    3 LLSVNDRVLL--GDKFGTVRFIGKTKFKDGIWIGLELDDPVGKNDGSVNGVRYFHCKKRHGIFIRP 66
NIP100 COG5244
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ...
 176-236 3.54e-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: 3.54e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767915242 176 LKLGDRVVIaGQKVGTLRFCGTTEFASGQWAGIELDEPEGKNNGSVGKVQYFKCAPKYGIF 236
Cdd:COG5244    4 LSVNDRVLL-GDKFGTVRFIGKTKFKDGIWIGLELDDPVGKNDGSVNGVRYFHCKKRHGIF 63
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-118 6.61e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 75.38  E-value: 6.61e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915242   1 MTLLHYtcksgAHGIGDVEtAVKFatqLIDLGADISLRSRWtNMNALHYAAYFDVPELIRVILKtsKPKDVDATcsDFNF 80
Cdd:COG0666  121 ETPLHL-----AAYNGNLE-IVKL---LLEAGADVNAQDND-GNTPLHLAAANGNLEIVKLLLE--AGADVNAR--DNDG 186

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 767915242  81 GTALHIAAYNLCAGAVKCLLEQGANPAFRNDKGQIPAD 118
Cdd:COG0666  187 ETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALD 224
Ank_2 pfam12796
Ankyrin repeats (3 copies);
4-110 1.18e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 55.51  E-value: 1.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915242    4 LHYTCKSGAHGIgdvetaVKFatqLIDLGADISLRSRWtNMNALHYAAYFDVPELIRVILKTskpKDVDATCSDFnfgTA 83
Cdd:pfam12796   1 LHLAAKNGNLEL------VKL---LLENGADANLQDKN-GRTALHLAAKNGHLEIVKLLLEH---ADVNLKDNGR---TA 64

                          90       100
                  ....*....|....*....|....*..
gi 767915242   84 LHIAAYNLCAGAVKCLLEQGANPAFRN 110
Cdd:pfam12796  65 LHYAARSGHLEIVKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 2-119 2.03e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 47.33  E-value: 2.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915242   2 TLLHYTCKsgahgigDVETAVKFatqLIDLGADISLRSRwTNMNALHYAAYFD-VPELIRVILKtskpKDVDATCSDFNF 80
Cdd:PHA03095  53 LYLHYSSE-------KVKDIVRL---LLEAGADVNAPER-CGFTPLHLYLYNAtTLDVIKLLIK----AGADVNAKDKVG 117

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 767915242  81 GTALHIAAYNLC--AGAVKCLLEQGANPAFRNDKGQIPADV 119
Cdd:PHA03095 118 RTPLHVYLSGFNinPKVIRLLLRKGADVNALDLYGMTPLAV 158
 
Name Accession Description Interval E-value
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 380-444 1.82e-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: 119.04  E-value: 1.82e-32
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767915242  380 LGERVLVVGQRLGTIRFFGTTNFAPGYWYGIELEKPHGKNDGSVGGVQYFSCSPRYGIFAPPSRV 444
Cdd:pfam01302   1 VGDRVEVPGGRRGTVRYVGPVPFAPGVWVGVELDEPVGKNDGSVKGVRYFECPPKHGVFVRPSKV 65
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 178-242 1.46e-31

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: 116.35  E-value: 1.46e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767915242  178 LGDRVVIAGQKVGTLRFCGTTEFASGQWAGIELDEPEGKNNGSVGKVQYFKCAPKYGIFAPLSKI 242
Cdd:pfam01302   1 VGDRVEVPGGRRGTVRYVGPVPFAPGVWVGVELDEPVGKNDGSVKGVRYFECPPKHGVFVRPSKV 65
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 519-583 4.36e-29

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: 109.41  E-value: 4.36e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767915242  519 GSQVLlTSSNEMGTVRYVGPTDFASGIWLGLELRSAKGKNDGSVGDKRYFTCKPNHGVLVRPSRV 583
Cdd:pfam01302   2 GDRVE-VPGGRRGTVRYVGPVPFAPGVWVGVELDEPVGKNDGSVKGVRYFECPPKHGVFVRPSKV 65
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
 178-243 3.17e-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: 107.29  E-value: 3.17e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767915242   178 LGDRV-VIAGQKVGTLRFCGTTEFASGQWAGIELDEPE-GKNNGSVGKVQYFKCAPKYGIFAPLSKIS 243
Cdd:smart01052   1 VGDRVeVGGGGRRGTVRYVGPTPFAPGVWVGVELDEPLrGKNDGSVKGVRYFECPPKHGIFVRPSKVE 68
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
 380-445 4.05e-27

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: 104.20  E-value: 4.05e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767915242   380 LGERVLVVG-QRLGTIRFFGTTNFAPGYWYGIELEKPH-GKNDGSVGGVQYFSCSPRYGIFAPPSRVQ 445
Cdd:smart01052   1 VGDRVEVGGgGRRGTVRYVGPTPFAPGVWVGVELDEPLrGKNDGSVKGVRYFECPPKHGIFVRPSKVE 68
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
 519-584 7.82e-27

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: 103.43  E-value: 7.82e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767915242   519 GSQVLLTSSNEMGTVRYVGPTDFASGIWLGLELR-SAKGKNDGSVGDKRYFTCKPNHGVLVRPSRVT 584
Cdd:smart01052   2 GDRVEVGGGGRRGTVRYVGPTPFAPGVWVGVELDePLRGKNDGSVKGVRYFECPPKHGIFVRPSKVE 68
NIP100 COG5244
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ...
 378-507 6.00e-18

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: 87.82  E-value: 6.00e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915242 378 LRLGERVLVvGQRLGTIRFFGTTNFAPGYWYGIELEKPHGKNDGSVGGVQYFSCSPRYGIFAPP--SRVQRVTDSLDTLS 455
Cdd:COG5244    4 LSVNDRVLL-GDKFGTVRFIGKTKFKDGIWIGLELDDPVGKNDGSVNGVRYFHCKKRHGIFIRPddDSLLNGNAAYEKIK 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767915242 456 EISSNKQNhsypgfrrSFSTTSASSQKEINRRNAFSKSKAalrRSWSSTPTA 507
Cdd:COG5244   83 GGLVCESK--------GMDKDGEIKQENHEDRIHFEESKI---RRLEETIEA 123
NIP100 COG5244
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ...
 515-580 2.17e-17

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: 85.89  E-value: 2.17e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767915242 515 KLHEGSQVLLtsSNEMGTVRYVGPTDFASGIWLGLELRSAKGKNDGSVGDKRYFTCKPNHGVLVRP 580
Cdd:COG5244    3 LLSVNDRVLL--GDKFGTVRFIGKTKFKDGIWIGLELDDPVGKNDGSVNGVRYFHCKKRHGIFIRP 66
NIP100 COG5244
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ...
 176-236 3.54e-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: 3.54e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767915242 176 LKLGDRVVIaGQKVGTLRFCGTTEFASGQWAGIELDEPEGKNNGSVGKVQYFKCAPKYGIF 236
Cdd:COG5244    4 LSVNDRVLL-GDKFGTVRFIGKTKFKDGIWIGLELDDPVGKNDGSVNGVRYFHCKKRHGIF 63
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-118 6.61e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 75.38  E-value: 6.61e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915242   1 MTLLHYtcksgAHGIGDVEtAVKFatqLIDLGADISLRSRWtNMNALHYAAYFDVPELIRVILKtsKPKDVDATcsDFNF 80
Cdd:COG0666  121 ETPLHL-----AAYNGNLE-IVKL---LLEAGADVNAQDND-GNTPLHLAAANGNLEIVKLLLE--AGADVNAR--DNDG 186

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 767915242  81 GTALHIAAYNLCAGAVKCLLEQGANPAFRNDKGQIPAD 118
Cdd:COG0666  187 ETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALD 224
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
2-118 6.72e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 63.43  E-value: 6.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915242   2 TLLHYTCKSGahgigDVEtAVKFatqLIDLGADISLRSRwTNMNALHYAAYFDVPELIRVILKtsKPKDVDATcsDFNFG 81
Cdd:COG0666  155 TPLHLAAANG-----NLE-IVKL---LLEAGADVNARDN-DGETPLHLAAENGHLEIVKLLLE--AGADVNAK--DNDGK 220

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 767915242  82 TALHIAAYNLCAGAVKCLLEQGANPAFRNDKGQIPAD 118
Cdd:COG0666  221 TALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALL 257
Ank_2 pfam12796
Ankyrin repeats (3 copies);
4-110 1.18e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 55.51  E-value: 1.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915242    4 LHYTCKSGAHGIgdvetaVKFatqLIDLGADISLRSRWtNMNALHYAAYFDVPELIRVILKTskpKDVDATCSDFnfgTA 83
Cdd:pfam12796   1 LHLAAKNGNLEL------VKL---LLENGADANLQDKN-GRTALHLAAKNGHLEIVKLLLEH---ADVNLKDNGR---TA 64

                          90       100
                  ....*....|....*....|....*..
gi 767915242   84 LHIAAYNLCAGAVKCLLEQGANPAFRN 110
Cdd:pfam12796  65 LHYAARSGHLEIVKLLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
25-147 2.75e-08

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 55.73  E-value: 2.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915242  25 ATQLIDLGADISLRSRWTNMNALHYAAYFDVPELIRVILKtsKPKDVDATcsDFNFGTALHIAAYNLCAGAVKCLLEQGA 104
Cdd:COG0666   69 VALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLE--AGADVNAR--DKDGETPLHLAAYNGNLEIVKLLLEAGA 144

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 767915242 105 NPAFRNDKGQipadvvpdpvdMPLEMAdAAATAKEIKQMLLDA 147
Cdd:COG0666  145 DVNAQDNDGN-----------TPLHLA-AANGNLEIVKLLLEA 175
PHA03095 PHA03095
ankyrin-like protein; Provisional
 2-119 2.03e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 47.33  E-value: 2.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915242   2 TLLHYTCKsgahgigDVETAVKFatqLIDLGADISLRSRwTNMNALHYAAYFD-VPELIRVILKtskpKDVDATCSDFNF 80
Cdd:PHA03095  53 LYLHYSSE-------KVKDIVRL---LLEAGADVNAPER-CGFTPLHLYLYNAtTLDVIKLLIK----AGADVNAKDKVG 117

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 767915242  81 GTALHIAAYNLC--AGAVKCLLEQGANPAFRNDKGQIPADV 119
Cdd:PHA03095 118 RTPLHVYLSGFNinPKVIRLLLRKGADVNALDLYGMTPLAV 158
Ank_4 pfam13637
Ankyrin repeats (many copies);
43-100 4.89e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.11  E-value: 4.89e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767915242   43 NMNALHYAAYFDVPELIRVILKtsKPKDVDATCSDFNfgTALHIAAYNLCAGAVKCLL 100
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLE--KGADINAVDGNGE--TALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 28-149 7.30e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 42.34  E-value: 7.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915242  28 LIDLGADISLrSRWTNMNALHYAAYFDVPELirVILKT--SKPKDVDATCS--------------DFNFGTALHIAAYNL 91
Cdd:PHA03100 127 LLDNGANVNI-KNSDGENLLHLYLESNKIDL--KILKLliDKGVDINAKNRvnyllsygvpinikDVYGFTPLHYAVYNN 203

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767915242  92 CAGAVKCLLEQGANPAFRNDKGqipadvvpdpvDMPLEMAdAAATAKEIKQMLLDAVP 149
Cdd:PHA03100 204 NPEFVKYLLDLGANPNLVNKYG-----------DTPLHIA-ILNNNKEIFKLLLNNGP 249
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-113 9.07e-04

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 41.48  E-value: 9.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915242   1 MTLLHYTCKSGAHGIgdvetaVKFatqLIDLGADISLRSRWtNMNALHYAAYFDVPELIRVILKTSKPKDVDatcsDFNF 80
Cdd:COG0666  187 ETPLHLAAENGHLEI------VKL---LLEAGADVNAKDND-GKTALDLAAENGNLEIVKLLLEAGADLNAK----DKDG 252

                         90       100       110
                 ....*....|....*....|....*....|...
gi 767915242  81 GTALHIAAYNLCAGAVKCLLEQGANPAFRNDKG 113
Cdd:COG0666  253 LTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285
 
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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