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Conserved domains on  [gi|407892485|ref|NP_001258412|]
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CAP-Gly domain-containing linker protein 4 isoform 3 [Mus musculus]

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 ...
 486-550 2.06e-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: 119.43  E-value: 2.06e-32
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 407892485  486 LGERVLVVGQRVGTIKFFGTTNFAPGYWYGIELEKPHGKNDGSVGGVQYFSCSPRYGIFAPPSRV 550
Cdd:pfam01302   1 VGDRVEVPGGRRGTVRYVGPVPFAPGVWVGVELDEPVGKNDGSVKGVRYFECPPKHGVFVRPSKV 65
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 285-349 1.17e-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: 117.12  E-value: 1.17e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 407892485  285 LGDRVVIAGQKVGTLRFCGTTEFASGQWAGIELDEPEGKNNGSVGRVQYFKCAPKYGIFAPLSKI 349
Cdd:pfam01302   1 VGDRVEVPGGRRGTVRYVGPVPFAPGVWVGVELDEPVGKNDGSVKGVRYFECPPKHGVFVRPSKV 65
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
84-254 8.73e-17

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 81.54  E-value: 8.73e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407892485  84 NIDIIgNEILKRGCNVNDRDGLtDMTLLHYtcksgAHGIGDIEtAVKFaaqLIDLGADASLRSRWtNMNALHYASYFDVP 163
Cdd:COG0666   99 DLEIV-KLLLEAGADVNARDKD-GETPLHL-----AAYNGNLE-IVKL---LLEAGADVNAQDND-GNTPLHLAAANGNL 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407892485 164 ELIRVILKtsKPKDVDATcsDFNFGTALHIAAHNLCAGAVKTLLELGANPAFRNDKGQIPAevvpdpvdmpleMADAAAI 243
Cdd:COG0666  167 EIVKLLLE--AGADVNAR--DNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTAL------------DLAAENG 230

                        170
                 ....*....|.
gi 407892485 244 AKEIKQMLLDA 254
Cdd:COG0666  231 NLEIVKLLLEA 241
 
Name Accession Description Interval E-value
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 486-550 2.06e-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: 119.43  E-value: 2.06e-32
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 407892485  486 LGERVLVVGQRVGTIKFFGTTNFAPGYWYGIELEKPHGKNDGSVGGVQYFSCSPRYGIFAPPSRV 550
Cdd:pfam01302   1 VGDRVEVPGGRRGTVRYVGPVPFAPGVWVGVELDEPVGKNDGSVKGVRYFECPPKHGVFVRPSKV 65
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 285-349 1.17e-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: 117.12  E-value: 1.17e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 407892485  285 LGDRVVIAGQKVGTLRFCGTTEFASGQWAGIELDEPEGKNNGSVGRVQYFKCAPKYGIFAPLSKI 349
Cdd:pfam01302   1 VGDRVEVPGGRRGTVRYVGPVPFAPGVWVGVELDEPVGKNDGSVKGVRYFECPPKHGVFVRPSKV 65
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
 285-350 3.07e-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: 3.07e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 407892485   285 LGDRV-VIAGQKVGTLRFCGTTEFASGQWAGIELDEPE-GKNNGSVGRVQYFKCAPKYGIFAPLSKIS 350
Cdd:smart01052   1 VGDRVeVGGGGRRGTVRYVGPTPFAPGVWVGVELDEPLrGKNDGSVKGVRYFECPPKHGIFVRPSKVE 68
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
 486-551 1.77e-26

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: 102.66  E-value: 1.77e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 407892485   486 LGERVLVVG-QRVGTIKFFGTTNFAPGYWYGIELEKPH-GKNDGSVGGVQYFSCSPRYGIFAPPSRVQ 551
Cdd:smart01052   1 VGDRVEVGGgGRRGTVRYVGPTPFAPGVWVGVELDEPLrGKNDGSVKGVRYFECPPKHGIFVRPSKVE 68
NIP100 COG5244
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ...
 484-547 6.56e-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: 84.74  E-value: 6.56e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 407892485 484 LHLGERVLVvGQRVGTIKFFGTTNFAPGYWYGIELEKPHGKNDGSVGGVQYFSCSPRYGIFAPP 547
Cdd:COG5244    4 LSVNDRVLL-GDKFGTVRFIGKTKFKDGIWIGLELDDPVGKNDGSVNGVRYFHCKKRHGIFIRP 66
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
84-254 8.73e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 81.54  E-value: 8.73e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407892485  84 NIDIIgNEILKRGCNVNDRDGLtDMTLLHYtcksgAHGIGDIEtAVKFaaqLIDLGADASLRSRWtNMNALHYASYFDVP 163
Cdd:COG0666   99 DLEIV-KLLLEAGADVNARDKD-GETPLHL-----AAYNGNLE-IVKL---LLEAGADVNAQDND-GNTPLHLAAANGNL 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407892485 164 ELIRVILKtsKPKDVDATcsDFNFGTALHIAAHNLCAGAVKTLLELGANPAFRNDKGQIPAevvpdpvdmpleMADAAAI 243
Cdd:COG0666  167 EIVKLLLE--AGADVNAR--DNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTAL------------DLAAENG 230

                        170
                 ....*....|.
gi 407892485 244 AKEIKQMLLDA 254
Cdd:COG0666  231 NLEIVKLLLEA 241
NIP100 COG5244
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ...
 283-343 6.06e-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: 78.57  E-value: 6.06e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 407892485 283 LKLGDRVVIaGQKVGTLRFCGTTEFASGQWAGIELDEPEGKNNGSVGRVQYFKCAPKYGIF 343
Cdd:COG5244    4 LSVNDRVLL-GDKFGTVRFIGKTKFKDGIWIGLELDDPVGKNDGSVNGVRYFHCKKRHGIF 63
Ank_2 pfam12796
Ankyrin repeats (3 copies);
111-217 2.10e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 54.74  E-value: 2.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407892485  111 LHYTCKSGAHGIgdietaVKFaaqLIDLGADASLRSRWtNMNALHYASYFDVPELIRVILKTskpKDVDATCSDFnfgTA 190
Cdd:pfam12796   1 LHLAAKNGNLEL------VKL---LLENGADANLQDKN-GRTALHLAAKNGHLEIVKLLLEH---ADVNLKDNGR---TA 64

                          90       100
                  ....*....|....*....|....*..
gi 407892485  191 LHIAAHNLCAGAVKTLLELGANPAFRN 217
Cdd:pfam12796  65 LHYAARSGHLEIVKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 92-226 8.22e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 51.95  E-value: 8.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407892485  92 ILKRGCNVNDRDGLtDMTLLHYTCKSGAHGIGDIetaVKFaaqLIDLGADASLRSRwTNMNALH-YASYFDVPELIRVIL 170
Cdd:PHA03095  33 LLAAGADVNFRGEY-GKTPLHLYLHYSSEKVKDI---VRL---LLEAGADVNAPER-CGFTPLHlYLYNATTLDVIKLLI 104

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 407892485 171 KtskpKDVDATCSDFNFGTALHIAAHNLC--AGAVKTLLELGANPAFRNDKGQIPAEV 226
Cdd:PHA03095 105 K----AGADVNAKDKVGRTPLHVYLSGFNinPKVIRLLLRKGADVNALDLYGMTPLAV 158
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 152-212 7.98e-03

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 39.68  E-value: 7.98e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407892485  152 NALHYAS--YFDVPELIRVILKTSKPKD------VDATCSDFNFG-TALHIAAHNLCAGAVKTLLELGAN 212
Cdd:TIGR00870  84 TLLHAISleYVDAVEAILLHLLAAFRKSgplelaNDQYTSEFTPGiTALHLAAHRQNYEIVKLLLERGAS 153
 
Name Accession Description Interval E-value
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 486-550 2.06e-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: 119.43  E-value: 2.06e-32
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 407892485  486 LGERVLVVGQRVGTIKFFGTTNFAPGYWYGIELEKPHGKNDGSVGGVQYFSCSPRYGIFAPPSRV 550
Cdd:pfam01302   1 VGDRVEVPGGRRGTVRYVGPVPFAPGVWVGVELDEPVGKNDGSVKGVRYFECPPKHGVFVRPSKV 65
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 285-349 1.17e-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: 117.12  E-value: 1.17e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 407892485  285 LGDRVVIAGQKVGTLRFCGTTEFASGQWAGIELDEPEGKNNGSVGRVQYFKCAPKYGIFAPLSKI 349
Cdd:pfam01302   1 VGDRVEVPGGRRGTVRYVGPVPFAPGVWVGVELDEPVGKNDGSVKGVRYFECPPKHGVFVRPSKV 65
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
 285-350 3.07e-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: 3.07e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 407892485   285 LGDRV-VIAGQKVGTLRFCGTTEFASGQWAGIELDEPE-GKNNGSVGRVQYFKCAPKYGIFAPLSKIS 350
Cdd:smart01052   1 VGDRVeVGGGGRRGTVRYVGPTPFAPGVWVGVELDEPLrGKNDGSVKGVRYFECPPKHGIFVRPSKVE 68
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
 486-551 1.77e-26

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: 102.66  E-value: 1.77e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 407892485   486 LGERVLVVG-QRVGTIKFFGTTNFAPGYWYGIELEKPH-GKNDGSVGGVQYFSCSPRYGIFAPPSRVQ 551
Cdd:smart01052   1 VGDRVEVGGgGRRGTVRYVGPTPFAPGVWVGVELDEPLrGKNDGSVKGVRYFECPPKHGIFVRPSKVE 68
NIP100 COG5244
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ...
 484-547 6.56e-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: 84.74  E-value: 6.56e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 407892485 484 LHLGERVLVvGQRVGTIKFFGTTNFAPGYWYGIELEKPHGKNDGSVGGVQYFSCSPRYGIFAPP 547
Cdd:COG5244    4 LSVNDRVLL-GDKFGTVRFIGKTKFKDGIWIGLELDDPVGKNDGSVNGVRYFHCKKRHGIFIRP 66
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
84-254 8.73e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 81.54  E-value: 8.73e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407892485  84 NIDIIgNEILKRGCNVNDRDGLtDMTLLHYtcksgAHGIGDIEtAVKFaaqLIDLGADASLRSRWtNMNALHYASYFDVP 163
Cdd:COG0666   99 DLEIV-KLLLEAGADVNARDKD-GETPLHL-----AAYNGNLE-IVKL---LLEAGADVNAQDND-GNTPLHLAAANGNL 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407892485 164 ELIRVILKtsKPKDVDATcsDFNFGTALHIAAHNLCAGAVKTLLELGANPAFRNDKGQIPAevvpdpvdmpleMADAAAI 243
Cdd:COG0666  167 EIVKLLLE--AGADVNAR--DNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTAL------------DLAAENG 230

                        170
                 ....*....|.
gi 407892485 244 AKEIKQMLLDA 254
Cdd:COG0666  231 NLEIVKLLLEA 241
NIP100 COG5244
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ...
 283-343 6.06e-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: 78.57  E-value: 6.06e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 407892485 283 LKLGDRVVIaGQKVGTLRFCGTTEFASGQWAGIELDEPEGKNNGSVGRVQYFKCAPKYGIF 343
Cdd:COG5244    4 LSVNDRVLL-GDKFGTVRFIGKTKFKDGIWIGLELDDPVGKNDGSVNGVRYFHCKKRHGIF 63
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
84-254 1.33e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 68.83  E-value: 1.33e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407892485  84 NIDIIgNEILKRGCNVNDRDGlTDMTLLHYTCKSGahgigDIEtAVKFaaqLIDLGADASLRSRwTNMNALHYASYFDVP 163
Cdd:COG0666  132 NLEIV-KLLLEAGADVNAQDN-DGNTPLHLAAANG-----NLE-IVKL---LLEAGADVNARDN-DGETPLHLAAENGHL 199

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407892485 164 ELIRVILKtsKPKDVDATcsDFNFGTALHIAAHNLCAGAVKTLLELGANPAFRNDKGQIPAEVVPDPVDMPLEMADAAAI 243
Cdd:COG0666  200 EIVKLLLE--AGADVNAK--DNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLAL 275

                        170
                 ....*....|.
gi 407892485 244 AKEIKQMLLDA 254
Cdd:COG0666  276 LLLAAALLDLL 286
Ank_2 pfam12796
Ankyrin repeats (3 copies);
111-217 2.10e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 54.74  E-value: 2.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407892485  111 LHYTCKSGAHGIgdietaVKFaaqLIDLGADASLRSRWtNMNALHYASYFDVPELIRVILKTskpKDVDATCSDFnfgTA 190
Cdd:pfam12796   1 LHLAAKNGNLEL------VKL---LLENGADANLQDKN-GRTALHLAAKNGHLEIVKLLLEH---ADVNLKDNGR---TA 64

                          90       100
                  ....*....|....*....|....*..
gi 407892485  191 LHIAAHNLCAGAVKTLLELGANPAFRN 217
Cdd:pfam12796  65 LHYAARSGHLEIVKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 92-226 8.22e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 51.95  E-value: 8.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407892485  92 ILKRGCNVNDRDGLtDMTLLHYTCKSGAHGIGDIetaVKFaaqLIDLGADASLRSRwTNMNALH-YASYFDVPELIRVIL 170
Cdd:PHA03095  33 LLAAGADVNFRGEY-GKTPLHLYLHYSSEKVKDI---VRL---LLEAGADVNAPER-CGFTPLHlYLYNATTLDVIKLLI 104

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 407892485 171 KtskpKDVDATCSDFNFGTALHIAAHNLC--AGAVKTLLELGANPAFRNDKGQIPAEV 226
Cdd:PHA03095 105 K----AGADVNAKDKVGRTPLHVYLSGFNinPKVIRLLLRKGADVNALDLYGMTPLAV 158
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 92-225 3.87e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 46.58  E-value: 3.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407892485  92 ILKRGCNVNDRDGLTDMTLLHYTCKSgahgIGDIETaVKFaaqLIDLGADASLrSRWTNMNALHYASYFDVPELirVILK 171
Cdd:PHA03100  92 LLEYGANVNAPDNNGITPLLYAISKK----SNSYSI-VEY---LLDNGANVNI-KNSDGENLLHLYLESNKIDL--KILK 160

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407892485 172 T--SKPKDVDATCS--------------DFNFGTALHIAAHNLCAGAVKTLLELGANPAFRNDKGQIPAE 225
Cdd:PHA03100 161 LliDKGVDINAKNRvnyllsygvpinikDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLH 230
Ank_4 pfam13637
Ankyrin repeats (many copies);
150-207 6.66e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.02  E-value: 6.66e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 407892485  150 NMNALHYASYFDVPELIRVILKtsKPKDVDATCSDFNfgTALHIAAHNLCAGAVKTLL 207
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLE--KGADINAVDGNGE--TALHFAASNGNVEVLKLLL 54
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
132-254 1.75e-03

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 41.09  E-value: 1.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407892485 132 AAQLIDLGADASLRSRWTNMNALHYASYFDVPELIRVILKtskpKDVDATCSDFNFGTALHIAAHNLCAGAVKTLLELGA 211
Cdd:COG0666   36 LLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLA----AGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGA 111

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 407892485 212 NPAFRNDKGQIpaevvpdpvdmPLEMAdAAAIAKEIKQMLLDA 254
Cdd:COG0666  112 DVNARDKDGET-----------PLHLA-AYNGNLEIVKLLLEA 142
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 166-226 5.53e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 39.88  E-value: 5.53e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 407892485 166 IRVILKTSkpkdVDATCSDFNFGTALHIAAHNLCAGAVKTLLELGANPAFRNDKGQIPAEV 226
Cdd:PTZ00322  98 ARILLTGG----ADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLEL 154
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 152-212 7.98e-03

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 39.68  E-value: 7.98e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407892485  152 NALHYAS--YFDVPELIRVILKTSKPKD------VDATCSDFNFG-TALHIAAHNLCAGAVKTLLELGAN 212
Cdd:TIGR00870  84 TLLHAISleYVDAVEAILLHLLAAFRKSgplelaNDQYTSEFTPGiTALHLAAHRQNYEIVKLLLERGAS 153
 
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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