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Conserved domains on  [gi|18105054|ref|NP_055785|]
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kinesin-associated protein 3 isoform 1 [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 ...
13-720 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: 1244.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105054    13 VKGGNIDVHPSEKALIVHYEVEATILGEMGDPMLGERKECQKIIRLKSLNANTDITSLARKVVEECKLIHPSKLNEVEQL 92
Cdd:pfam05804   1 VKGGSIDVHPTEKALIVNYELEATILGEMGDPMLGERKECQKIIRLRSLNAKTDIAALAREVVEKCKLIHPSKLNEVEQL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105054    93 LYYLQNRRDSL--SGKEKKEKSSKPKDPPPFEGMEIDEVANINDMDEYIELLYEDIPDKVRGSALILQLARNPDNLEELL 170
Cdd:pfam05804  81 LYYLQNRKDSHtrSGARKHESVAKMKDPPPAEGPEADEVANINDIDEYIELLYEDLPEKVRGSALILQLARNPDNLEELE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105054   171 LNETALGALARVLREDWKQSVELATNIIYIFFCFSSFSQFHGLITHYKIGALCMNIIDHELKRHELWQEELSKKKKAVDE 250
Cdd:pfam05804 161 KNETCLGALARVLREDWKKSVELATNIIYIFFCFSSFSQFHPLIVHYKIGALCMDVIDHELKRHETWREELDKKKKMNEE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105054   251 DPENqtlRKDYEKTFKKYQGLVVKQEQLLRVALYLLLNLAEDTRTELKMRNKNIVHMLVKALDRDNFELLILVVSFLKKL 330
Cdd:pfam05804 241 KPIL---NSDYEKSLKKYKGLAKKQEQLLRVAFYLLLNLAEDVKLELKMRNKNIVKMLVKALDRDNIELLILVVSFLKKL 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105054   331 SIFMENKNDMVEMDIVEKLVKMIPCEHEDLLNITLRLLLNLSFDTGLRNKMVQVGLLPKLTALLGNDNYKQIAMCVLYHI 410
Cdd:pfam05804 318 SIVGENKNEMGELNIVEKLPKLFPCTHEDLLNITLRLLLNLSFDTGLRRKMIAAGYLPKLVMLLNNDNHHGIAVCVLYHM 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105054   411 SMDDRFKSMFAYTDCIPQLMKMLFECSDERIDLELISFCINLAANKRNVQLICEGNGLKMLMKRALKFKDPLLMKMIRNI 490
Cdd:pfam05804 398 SLDDKVKSMFTYTDCIPMAMKMIIENLNERVDLELIALCINLALNKRNAQLICEGNGLHSLMDRALKFQDPLLMKMIRNI 477
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105054   491 SQHDGPTKNLFIDYVGDLAAQISNDEEEEFVIECLGTLANLTIPDLDWELVLKEYKLVPYLKDKLKPGAAEDDLVLEVVI 570
Cdd:pfam05804 478 SQHDGPLKLQFIDYVGDLARIITICDDEEFVVECLGILANLTIPDLDYEQILQEFQLVPWIKQKLLPGAAEDDLVLEVVV 557
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105054   571 MIGTVSMDDSCAALLAKSGIIPALIELLNAQQEDDEFVCQIIYVFYQMVFHQATRDVIIKETQAPAYLIDLMHDKNNEIR 650
Cdd:pfam05804 558 YLGTVACDDSCAALLAKSGIIISLIELLNAKQEDDEIVCQIIYVFYQMVFHEATREVIIKETQAPAYLIDLMHDKNEEIR 637
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18105054   651 KVCDNTLDIIAEYDEEWAKKIQSEKFRWHNSQWLEMVESRQMDESEQYL-YGDDRIEPYIHEGDILERPDL 720
Cdd:pfam05804 638 KVCDNTLDIIAESDEEWAKKIKLEKFRWHNSQWLEMVESQQDDDNEQGLdYGDQEDEPYILESDILDRPDL 708
 
Name Accession Description Interval E-value
KAP pfam05804
Kinesin-associated protein (KAP); This family consists of several eukaryotic ...
13-720 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: 1244.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105054    13 VKGGNIDVHPSEKALIVHYEVEATILGEMGDPMLGERKECQKIIRLKSLNANTDITSLARKVVEECKLIHPSKLNEVEQL 92
Cdd:pfam05804   1 VKGGSIDVHPTEKALIVNYELEATILGEMGDPMLGERKECQKIIRLRSLNAKTDIAALAREVVEKCKLIHPSKLNEVEQL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105054    93 LYYLQNRRDSL--SGKEKKEKSSKPKDPPPFEGMEIDEVANINDMDEYIELLYEDIPDKVRGSALILQLARNPDNLEELL 170
Cdd:pfam05804  81 LYYLQNRKDSHtrSGARKHESVAKMKDPPPAEGPEADEVANINDIDEYIELLYEDLPEKVRGSALILQLARNPDNLEELE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105054   171 LNETALGALARVLREDWKQSVELATNIIYIFFCFSSFSQFHGLITHYKIGALCMNIIDHELKRHELWQEELSKKKKAVDE 250
Cdd:pfam05804 161 KNETCLGALARVLREDWKKSVELATNIIYIFFCFSSFSQFHPLIVHYKIGALCMDVIDHELKRHETWREELDKKKKMNEE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105054   251 DPENqtlRKDYEKTFKKYQGLVVKQEQLLRVALYLLLNLAEDTRTELKMRNKNIVHMLVKALDRDNFELLILVVSFLKKL 330
Cdd:pfam05804 241 KPIL---NSDYEKSLKKYKGLAKKQEQLLRVAFYLLLNLAEDVKLELKMRNKNIVKMLVKALDRDNIELLILVVSFLKKL 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105054   331 SIFMENKNDMVEMDIVEKLVKMIPCEHEDLLNITLRLLLNLSFDTGLRNKMVQVGLLPKLTALLGNDNYKQIAMCVLYHI 410
Cdd:pfam05804 318 SIVGENKNEMGELNIVEKLPKLFPCTHEDLLNITLRLLLNLSFDTGLRRKMIAAGYLPKLVMLLNNDNHHGIAVCVLYHM 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105054   411 SMDDRFKSMFAYTDCIPQLMKMLFECSDERIDLELISFCINLAANKRNVQLICEGNGLKMLMKRALKFKDPLLMKMIRNI 490
Cdd:pfam05804 398 SLDDKVKSMFTYTDCIPMAMKMIIENLNERVDLELIALCINLALNKRNAQLICEGNGLHSLMDRALKFQDPLLMKMIRNI 477
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105054   491 SQHDGPTKNLFIDYVGDLAAQISNDEEEEFVIECLGTLANLTIPDLDWELVLKEYKLVPYLKDKLKPGAAEDDLVLEVVI 570
Cdd:pfam05804 478 SQHDGPLKLQFIDYVGDLARIITICDDEEFVVECLGILANLTIPDLDYEQILQEFQLVPWIKQKLLPGAAEDDLVLEVVV 557
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105054   571 MIGTVSMDDSCAALLAKSGIIPALIELLNAQQEDDEFVCQIIYVFYQMVFHQATRDVIIKETQAPAYLIDLMHDKNNEIR 650
Cdd:pfam05804 558 YLGTVACDDSCAALLAKSGIIISLIELLNAKQEDDEIVCQIIYVFYQMVFHEATREVIIKETQAPAYLIDLMHDKNEEIR 637
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18105054   651 KVCDNTLDIIAEYDEEWAKKIQSEKFRWHNSQWLEMVESRQMDESEQYL-YGDDRIEPYIHEGDILERPDL 720
Cdd:pfam05804 638 KVCDNTLDIIAESDEEWAKKIKLEKFRWHNSQWLEMVESQQDDDNEQGLdYGDQEDEPYILESDILDRPDL 708
PRK05377 PRK05377
fructose-1,6-bisphosphate aldolase; Reviewed
560-607 5.54e-03

fructose-1,6-bisphosphate aldolase; Reviewed


Pssm-ID: 180045  Cd Length: 296  Bit Score: 39.47  E-value: 5.54e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 18105054  560 AEDDLVLEVVIMIGTVSMDDSCAALLAKSGIIP----ALIELLNAQQEDDEF 607
Cdd:PRK05377 228 IDHPRVLRVVALSGGYSRDEANELLARNHGLIAsfsrALTEGLSAQQSDEEF 279
 
Name Accession Description Interval E-value
KAP pfam05804
Kinesin-associated protein (KAP); This family consists of several eukaryotic ...
13-720 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: 1244.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105054    13 VKGGNIDVHPSEKALIVHYEVEATILGEMGDPMLGERKECQKIIRLKSLNANTDITSLARKVVEECKLIHPSKLNEVEQL 92
Cdd:pfam05804   1 VKGGSIDVHPTEKALIVNYELEATILGEMGDPMLGERKECQKIIRLRSLNAKTDIAALAREVVEKCKLIHPSKLNEVEQL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105054    93 LYYLQNRRDSL--SGKEKKEKSSKPKDPPPFEGMEIDEVANINDMDEYIELLYEDIPDKVRGSALILQLARNPDNLEELL 170
Cdd:pfam05804  81 LYYLQNRKDSHtrSGARKHESVAKMKDPPPAEGPEADEVANINDIDEYIELLYEDLPEKVRGSALILQLARNPDNLEELE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105054   171 LNETALGALARVLREDWKQSVELATNIIYIFFCFSSFSQFHGLITHYKIGALCMNIIDHELKRHELWQEELSKKKKAVDE 250
Cdd:pfam05804 161 KNETCLGALARVLREDWKKSVELATNIIYIFFCFSSFSQFHPLIVHYKIGALCMDVIDHELKRHETWREELDKKKKMNEE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105054   251 DPENqtlRKDYEKTFKKYQGLVVKQEQLLRVALYLLLNLAEDTRTELKMRNKNIVHMLVKALDRDNFELLILVVSFLKKL 330
Cdd:pfam05804 241 KPIL---NSDYEKSLKKYKGLAKKQEQLLRVAFYLLLNLAEDVKLELKMRNKNIVKMLVKALDRDNIELLILVVSFLKKL 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105054   331 SIFMENKNDMVEMDIVEKLVKMIPCEHEDLLNITLRLLLNLSFDTGLRNKMVQVGLLPKLTALLGNDNYKQIAMCVLYHI 410
Cdd:pfam05804 318 SIVGENKNEMGELNIVEKLPKLFPCTHEDLLNITLRLLLNLSFDTGLRRKMIAAGYLPKLVMLLNNDNHHGIAVCVLYHM 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105054   411 SMDDRFKSMFAYTDCIPQLMKMLFECSDERIDLELISFCINLAANKRNVQLICEGNGLKMLMKRALKFKDPLLMKMIRNI 490
Cdd:pfam05804 398 SLDDKVKSMFTYTDCIPMAMKMIIENLNERVDLELIALCINLALNKRNAQLICEGNGLHSLMDRALKFQDPLLMKMIRNI 477
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105054   491 SQHDGPTKNLFIDYVGDLAAQISNDEEEEFVIECLGTLANLTIPDLDWELVLKEYKLVPYLKDKLKPGAAEDDLVLEVVI 570
Cdd:pfam05804 478 SQHDGPLKLQFIDYVGDLARIITICDDEEFVVECLGILANLTIPDLDYEQILQEFQLVPWIKQKLLPGAAEDDLVLEVVV 557
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105054   571 MIGTVSMDDSCAALLAKSGIIPALIELLNAQQEDDEFVCQIIYVFYQMVFHQATRDVIIKETQAPAYLIDLMHDKNNEIR 650
Cdd:pfam05804 558 YLGTVACDDSCAALLAKSGIIISLIELLNAKQEDDEIVCQIIYVFYQMVFHEATREVIIKETQAPAYLIDLMHDKNEEIR 637
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18105054   651 KVCDNTLDIIAEYDEEWAKKIQSEKFRWHNSQWLEMVESRQMDESEQYL-YGDDRIEPYIHEGDILERPDL 720
Cdd:pfam05804 638 KVCDNTLDIIAESDEEWAKKIKLEKFRWHNSQWLEMVESQQDDDNEQGLdYGDQEDEPYILESDILDRPDL 708
PRK05377 PRK05377
fructose-1,6-bisphosphate aldolase; Reviewed
560-607 5.54e-03

fructose-1,6-bisphosphate aldolase; Reviewed


Pssm-ID: 180045  Cd Length: 296  Bit Score: 39.47  E-value: 5.54e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 18105054  560 AEDDLVLEVVIMIGTVSMDDSCAALLAKSGIIP----ALIELLNAQQEDDEF 607
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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