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Conserved domains on  [gi|119611275|gb|EAW90869|]
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kinesin-associated protein 3, isoform CRA_a, partial [Homo sapiens]

Protein Classification

KAP domain-containing protein( domain architecture ID 12066124)

KAP domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
KAP pfam05804
Kinesin-associated protein (KAP); This family consists of several eukaryotic ...
13-727 0e+00

Kinesin-associated protein (KAP); This family consists of several eukaryotic kinesin-associated (KAP) proteins. Kinesins are intracellular multimeric transport motor proteins that move cellular cargo on microtubule tracks. It has been shown that the sea urchin KRP85/95 holoenzyme associates with a KAP115 non-motor protein, forming a heterotrimeric complex in vitro, called the Kinesin-II. It includes kinesin-associated protein 3 (KAP3, also known as SMAP). In human and mouse, KAP3 is involved in tethering the chromosomes to the spindle pole and in chromosome movement. It binds to the tail domain of the KIF3A/KIF3B heterodimer to form a heterotrimeric KIF3 complex and may regulate the membrane binding of this complex.


:

Pssm-ID: 253396 [Multi-domain]  Cd Length: 708  Bit Score: 1233.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611275   13 VKGGNIDVHPSEKALIVHYEVEATILGEMGDPMLGERKECQKIIRLKSLNANTDITSLARKVVEECKLIHPSKLNEVEQL 92
Cdd:pfam05804   1 VKGGSIDVHPTEKALIVNYELEATILGEMGDPMLGERKECQKIIRLRSLNAKTDIAALAREVVEKCKLIHPSKLNEVEQL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611275   93 LYYLQNRRDSL--SGKEKKEKSSKPKDPPPFEGMEIDEVANINDMDEYIELLYEDIPDKVRGSALILQLARNPDNLEELL 170
Cdd:pfam05804  81 LYYLQNRKDSHtrSGARKHESVAKMKDPPPAEGPEADEVANINDIDEYIELLYEDLPEKVRGSALILQLARNPDNLEELE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611275  171 LNETALGALARVLREDWKQSVELATNIIYIFFCFSSFSQFHGLITHYKIGALCMNIIDHELKRHELWQEELSKKKKADil 250
Cdd:pfam05804 161 KNETCLGALARVLREDWKKSVELATNIIYIFFCFSSFSQFHPLIVHYKIGALCMDVIDHELKRHETWREELDKKKKMN-- 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611275  251 ldcllDEDPENqtlRKDYEKTFKKYQGLVVKQEQLLRVALYLLLNLAEDTRTELKMRNKNIVHMLVKALDRDNFELLILV 330
Cdd:pfam05804 239 -----EEKPIL---NSDYEKSLKKYKGLAKKQEQLLRVAFYLLLNLAEDVKLELKMRNKNIVKMLVKALDRDNIELLILV 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611275  331 VSFLKKLSIFMENKNDMVEMDIVEKLVKMIPCEHEDLLNITLRLLLNLSFDTGLRNKMVQVGLLPKLTALLGNDNYKQIA 410
Cdd:pfam05804 311 VSFLKKLSIVGENKNEMGELNIVEKLPKLFPCTHEDLLNITLRLLLNLSFDTGLRRKMIAAGYLPKLVMLLNNDNHHGIA 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611275  411 MCVLYHISMDDRFKSMFAYTDCIPQLMKMLFECSDERIDLELISFCINLAANKRNVQLICEGNGLKMLMKRALKFKDPLL 490
Cdd:pfam05804 391 VCVLYHMSLDDKVKSMFTYTDCIPMAMKMIIENLNERVDLELIALCINLALNKRNAQLICEGNGLHSLMDRALKFQDPLL 470
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611275  491 MKMIRNISQHDGPTKNLFIDYVGDLAAQISNDEEEEFVIECLGTLANLTIPDLDWELVLKEYKLVPYLKDKLKPGAAEDD 570
Cdd:pfam05804 471 MKMIRNISQHDGPLKLQFIDYVGDLARIITICDDEEFVVECLGILANLTIPDLDYEQILQEFQLVPWIKQKLLPGAAEDD 550
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611275  571 LVLEVVIMIGTVSMDDSCAALLAKSGIIPALIELLNAQQEDDEFVCQIIYVFYQMVFHQATRDVIIKETQAPAYLIDLMH 650
Cdd:pfam05804 551 LVLEVVVYLGTVACDDSCAALLAKSGIIISLIELLNAKQEDDEIVCQIIYVFYQMVFHEATREVIIKETQAPAYLIDLMH 630
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119611275  651 DKNNEIRKVCDNTLDIIAEYDEEWAKKIQSEKFRWHNSQWLEMVESRQMDESEQYL-YGDDRIEPYIHEGDILERPDL 727
Cdd:pfam05804 631 DKNEEIRKVCDNTLDIIAESDEEWAKKIKLEKFRWHNSQWLEMVESQQDDDNEQGLdYGDQEDEPYILESDILDRPDL 708
 
Name Accession Description Interval E-value
KAP pfam05804
Kinesin-associated protein (KAP); This family consists of several eukaryotic ...
13-727 0e+00

Kinesin-associated protein (KAP); This family consists of several eukaryotic kinesin-associated (KAP) proteins. Kinesins are intracellular multimeric transport motor proteins that move cellular cargo on microtubule tracks. It has been shown that the sea urchin KRP85/95 holoenzyme associates with a KAP115 non-motor protein, forming a heterotrimeric complex in vitro, called the Kinesin-II. It includes kinesin-associated protein 3 (KAP3, also known as SMAP). In human and mouse, KAP3 is involved in tethering the chromosomes to the spindle pole and in chromosome movement. It binds to the tail domain of the KIF3A/KIF3B heterodimer to form a heterotrimeric KIF3 complex and may regulate the membrane binding of this complex.


Pssm-ID: 253396 [Multi-domain]  Cd Length: 708  Bit Score: 1233.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611275   13 VKGGNIDVHPSEKALIVHYEVEATILGEMGDPMLGERKECQKIIRLKSLNANTDITSLARKVVEECKLIHPSKLNEVEQL 92
Cdd:pfam05804   1 VKGGSIDVHPTEKALIVNYELEATILGEMGDPMLGERKECQKIIRLRSLNAKTDIAALAREVVEKCKLIHPSKLNEVEQL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611275   93 LYYLQNRRDSL--SGKEKKEKSSKPKDPPPFEGMEIDEVANINDMDEYIELLYEDIPDKVRGSALILQLARNPDNLEELL 170
Cdd:pfam05804  81 LYYLQNRKDSHtrSGARKHESVAKMKDPPPAEGPEADEVANINDIDEYIELLYEDLPEKVRGSALILQLARNPDNLEELE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611275  171 LNETALGALARVLREDWKQSVELATNIIYIFFCFSSFSQFHGLITHYKIGALCMNIIDHELKRHELWQEELSKKKKADil 250
Cdd:pfam05804 161 KNETCLGALARVLREDWKKSVELATNIIYIFFCFSSFSQFHPLIVHYKIGALCMDVIDHELKRHETWREELDKKKKMN-- 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611275  251 ldcllDEDPENqtlRKDYEKTFKKYQGLVVKQEQLLRVALYLLLNLAEDTRTELKMRNKNIVHMLVKALDRDNFELLILV 330
Cdd:pfam05804 239 -----EEKPIL---NSDYEKSLKKYKGLAKKQEQLLRVAFYLLLNLAEDVKLELKMRNKNIVKMLVKALDRDNIELLILV 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611275  331 VSFLKKLSIFMENKNDMVEMDIVEKLVKMIPCEHEDLLNITLRLLLNLSFDTGLRNKMVQVGLLPKLTALLGNDNYKQIA 410
Cdd:pfam05804 311 VSFLKKLSIVGENKNEMGELNIVEKLPKLFPCTHEDLLNITLRLLLNLSFDTGLRRKMIAAGYLPKLVMLLNNDNHHGIA 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611275  411 MCVLYHISMDDRFKSMFAYTDCIPQLMKMLFECSDERIDLELISFCINLAANKRNVQLICEGNGLKMLMKRALKFKDPLL 490
Cdd:pfam05804 391 VCVLYHMSLDDKVKSMFTYTDCIPMAMKMIIENLNERVDLELIALCINLALNKRNAQLICEGNGLHSLMDRALKFQDPLL 470
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611275  491 MKMIRNISQHDGPTKNLFIDYVGDLAAQISNDEEEEFVIECLGTLANLTIPDLDWELVLKEYKLVPYLKDKLKPGAAEDD 570
Cdd:pfam05804 471 MKMIRNISQHDGPLKLQFIDYVGDLARIITICDDEEFVVECLGILANLTIPDLDYEQILQEFQLVPWIKQKLLPGAAEDD 550
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611275  571 LVLEVVIMIGTVSMDDSCAALLAKSGIIPALIELLNAQQEDDEFVCQIIYVFYQMVFHQATRDVIIKETQAPAYLIDLMH 650
Cdd:pfam05804 551 LVLEVVVYLGTVACDDSCAALLAKSGIIISLIELLNAKQEDDEIVCQIIYVFYQMVFHEATREVIIKETQAPAYLIDLMH 630
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119611275  651 DKNNEIRKVCDNTLDIIAEYDEEWAKKIQSEKFRWHNSQWLEMVESRQMDESEQYL-YGDDRIEPYIHEGDILERPDL 727
Cdd:pfam05804 631 DKNEEIRKVCDNTLDIIAESDEEWAKKIKLEKFRWHNSQWLEMVESQQDDDNEQGLdYGDQEDEPYILESDILDRPDL 708
PRK05377 PRK05377
fructose-1,6-bisphosphate aldolase; Reviewed
567-614 5.45e-03

fructose-1,6-bisphosphate aldolase; Reviewed


Pssm-ID: 180045  Cd Length: 296  Bit Score: 39.47  E-value: 5.45e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 119611275 567 AEDDLVLEVVIMIGTVSMDDSCAALLAKSGIIP----ALIELLNAQQEDDEF 614
Cdd:PRK05377 228 IDHPRVLRVVALSGGYSRDEANELLARNHGLIAsfsrALTEGLSAQQSDEEF 279
 
Name Accession Description Interval E-value
KAP pfam05804
Kinesin-associated protein (KAP); This family consists of several eukaryotic ...
13-727 0e+00

Kinesin-associated protein (KAP); This family consists of several eukaryotic kinesin-associated (KAP) proteins. Kinesins are intracellular multimeric transport motor proteins that move cellular cargo on microtubule tracks. It has been shown that the sea urchin KRP85/95 holoenzyme associates with a KAP115 non-motor protein, forming a heterotrimeric complex in vitro, called the Kinesin-II. It includes kinesin-associated protein 3 (KAP3, also known as SMAP). In human and mouse, KAP3 is involved in tethering the chromosomes to the spindle pole and in chromosome movement. It binds to the tail domain of the KIF3A/KIF3B heterodimer to form a heterotrimeric KIF3 complex and may regulate the membrane binding of this complex.


Pssm-ID: 253396 [Multi-domain]  Cd Length: 708  Bit Score: 1233.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611275   13 VKGGNIDVHPSEKALIVHYEVEATILGEMGDPMLGERKECQKIIRLKSLNANTDITSLARKVVEECKLIHPSKLNEVEQL 92
Cdd:pfam05804   1 VKGGSIDVHPTEKALIVNYELEATILGEMGDPMLGERKECQKIIRLRSLNAKTDIAALAREVVEKCKLIHPSKLNEVEQL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611275   93 LYYLQNRRDSL--SGKEKKEKSSKPKDPPPFEGMEIDEVANINDMDEYIELLYEDIPDKVRGSALILQLARNPDNLEELL 170
Cdd:pfam05804  81 LYYLQNRKDSHtrSGARKHESVAKMKDPPPAEGPEADEVANINDIDEYIELLYEDLPEKVRGSALILQLARNPDNLEELE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611275  171 LNETALGALARVLREDWKQSVELATNIIYIFFCFSSFSQFHGLITHYKIGALCMNIIDHELKRHELWQEELSKKKKADil 250
Cdd:pfam05804 161 KNETCLGALARVLREDWKKSVELATNIIYIFFCFSSFSQFHPLIVHYKIGALCMDVIDHELKRHETWREELDKKKKMN-- 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611275  251 ldcllDEDPENqtlRKDYEKTFKKYQGLVVKQEQLLRVALYLLLNLAEDTRTELKMRNKNIVHMLVKALDRDNFELLILV 330
Cdd:pfam05804 239 -----EEKPIL---NSDYEKSLKKYKGLAKKQEQLLRVAFYLLLNLAEDVKLELKMRNKNIVKMLVKALDRDNIELLILV 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611275  331 VSFLKKLSIFMENKNDMVEMDIVEKLVKMIPCEHEDLLNITLRLLLNLSFDTGLRNKMVQVGLLPKLTALLGNDNYKQIA 410
Cdd:pfam05804 311 VSFLKKLSIVGENKNEMGELNIVEKLPKLFPCTHEDLLNITLRLLLNLSFDTGLRRKMIAAGYLPKLVMLLNNDNHHGIA 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611275  411 MCVLYHISMDDRFKSMFAYTDCIPQLMKMLFECSDERIDLELISFCINLAANKRNVQLICEGNGLKMLMKRALKFKDPLL 490
Cdd:pfam05804 391 VCVLYHMSLDDKVKSMFTYTDCIPMAMKMIIENLNERVDLELIALCINLALNKRNAQLICEGNGLHSLMDRALKFQDPLL 470
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611275  491 MKMIRNISQHDGPTKNLFIDYVGDLAAQISNDEEEEFVIECLGTLANLTIPDLDWELVLKEYKLVPYLKDKLKPGAAEDD 570
Cdd:pfam05804 471 MKMIRNISQHDGPLKLQFIDYVGDLARIITICDDEEFVVECLGILANLTIPDLDYEQILQEFQLVPWIKQKLLPGAAEDD 550
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611275  571 LVLEVVIMIGTVSMDDSCAALLAKSGIIPALIELLNAQQEDDEFVCQIIYVFYQMVFHQATRDVIIKETQAPAYLIDLMH 650
Cdd:pfam05804 551 LVLEVVVYLGTVACDDSCAALLAKSGIIISLIELLNAKQEDDEIVCQIIYVFYQMVFHEATREVIIKETQAPAYLIDLMH 630
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119611275  651 DKNNEIRKVCDNTLDIIAEYDEEWAKKIQSEKFRWHNSQWLEMVESRQMDESEQYL-YGDDRIEPYIHEGDILERPDL 727
Cdd:pfam05804 631 DKNEEIRKVCDNTLDIIAESDEEWAKKIKLEKFRWHNSQWLEMVESQQDDDNEQGLdYGDQEDEPYILESDILDRPDL 708
PRK05377 PRK05377
fructose-1,6-bisphosphate aldolase; Reviewed
567-614 5.45e-03

fructose-1,6-bisphosphate aldolase; Reviewed


Pssm-ID: 180045  Cd Length: 296  Bit Score: 39.47  E-value: 5.45e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 119611275 567 AEDDLVLEVVIMIGTVSMDDSCAALLAKSGIIP----ALIELLNAQQEDDEF 614
Cdd:PRK05377 228 IDHPRVLRVVALSGGYSRDEANELLARNHGLIAsfsrALTEGLSAQQSDEEF 279
 
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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