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Conserved domains on  [gi|1823363439|ref|XP_032923322|]
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kinesin-associated protein 3 isoform X1 [Catharus ustulatus]

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 ...
13-721 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: 1280.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823363439  13 VKGGNIDVHPSEKALIVHYEVEATILGELGDPMLGERKECQKIIRLKSLNANTDIGSLARKVVEECKLIHPSKLAEVEQL 92
Cdd:pfam05804   1 VKGGSIDVHPTEKALIVNYELEATILGEMGDPMLGERKECQKIIRLRSLNAKTDIAALAREVVEKCKLIHPSKLNEVEQL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823363439  93 LYYLQNRRDS--SAGKEKKEKTSKPKDPPPFEGTEIDEVANINDMDEYIELLYEDIPDKVRGSALILQLARNPDNLEELL 170
Cdd:pfam05804  81 LYYLQNRKDShtRSGARKHESVAKMKDPPPAEGPEADEVANINDIDEYIELLYEDLPEKVRGSALILQLARNPDNLEELE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823363439 171 INETALGALARVLREDWKQSIELATNIIYIFFCFSSFTQFHGIITHYKIGALCMNIIDHELKRHELWQEELAKKKKAVDE 250
Cdd:pfam05804 161 KNETCLGALARVLREDWKKSVELATNIIYIFFCFSSFSQFHPLIVHYKIGALCMDVIDHELKRHETWREELDKKKKMNEE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823363439 251 DPENqtlKKDYEKTYKKYKGLVVKQEQLLRVAIYLLLNLAEDTRIELKMRNKNIVHMLVKALDRENFELLILVVTFLKKL 330
Cdd:pfam05804 241 KPIL---NSDYEKSLKKYKGLAKKQEQLLRVAFYLLLNLAEDVKLELKMRNKNIVKMLVKALDRDNIELLILVVSFLKKL 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823363439 331 SIFMENKNDMVEMDIVEKLVKMVPCEHEDLLNVTLRLLLNLSFDTGLRSKMVHVGLLPKLTALLGNENNKKVAICILYHI 410
Cdd:pfam05804 318 SIVGENKNEMGELNIVEKLPKLFPCTHEDLLNITLRLLLNLSFDTGLRRKMIAAGYLPKLVMLLNNDNHHGIAVCVLYHM 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823363439 411 SMDDCFKSMFAYTDCIPQLMKMLFECPDERVDLELISFCINLAANKRNVQLICEGNGLKMLMKRALKFKDPLLMKMIRNI 490
Cdd:pfam05804 398 SLDDKVKSMFTYTDCIPMAMKMIIENLNERVDLELIALCINLALNKRNAQLICEGNGLHSLMDRALKFQDPLLMKMIRNI 477
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823363439 491 SQHDGPTKSQFIEYVGDLAAQVSNDEEEEFVIECLGTLANLTLPELDWELVLKEYKLVPYLKDKLKPaGSAEDDLVLEVV 570
Cdd:pfam05804 478 SQHDGPLKLQFIDYVGDLARIITICDDEEFVVECLGILANLTIPDLDYEQILQEFQLVPWIKQKLLP-GAAEDDLVLEVV 556
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823363439 571 IMIGTVSMDDSCAALLAKSGIIPALIELLNAQQEDDEFVCQIIYVFYQMVFHQATRDVIIKETQAPAYLIDLMHDKNAEI 650
Cdd:pfam05804 557 VYLGTVACDDSCAALLAKSGIIISLIELLNAKQEDDEIVCQIIYVFYQMVFHEATREVIIKETQAPAYLIDLMHDKNEEI 636
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1823363439 651 RKVCDNTLDIIAEYDEEWAKKIQTEKFRWHNSQWLEMVESRQMDDSEQYL-YGDDPIEPYIHEGDILERPDL 721
Cdd:pfam05804 637 RKVCDNTLDIIAESDEEWAKKIKLEKFRWHNSQWLEMVESQQDDDNEQGLdYGDQEDEPYILESDILDRPDL 708
 
Name Accession Description Interval E-value
KAP pfam05804
Kinesin-associated protein (KAP); This family consists of several eukaryotic ...
13-721 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: 1280.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823363439  13 VKGGNIDVHPSEKALIVHYEVEATILGELGDPMLGERKECQKIIRLKSLNANTDIGSLARKVVEECKLIHPSKLAEVEQL 92
Cdd:pfam05804   1 VKGGSIDVHPTEKALIVNYELEATILGEMGDPMLGERKECQKIIRLRSLNAKTDIAALAREVVEKCKLIHPSKLNEVEQL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823363439  93 LYYLQNRRDS--SAGKEKKEKTSKPKDPPPFEGTEIDEVANINDMDEYIELLYEDIPDKVRGSALILQLARNPDNLEELL 170
Cdd:pfam05804  81 LYYLQNRKDShtRSGARKHESVAKMKDPPPAEGPEADEVANINDIDEYIELLYEDLPEKVRGSALILQLARNPDNLEELE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823363439 171 INETALGALARVLREDWKQSIELATNIIYIFFCFSSFTQFHGIITHYKIGALCMNIIDHELKRHELWQEELAKKKKAVDE 250
Cdd:pfam05804 161 KNETCLGALARVLREDWKKSVELATNIIYIFFCFSSFSQFHPLIVHYKIGALCMDVIDHELKRHETWREELDKKKKMNEE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823363439 251 DPENqtlKKDYEKTYKKYKGLVVKQEQLLRVAIYLLLNLAEDTRIELKMRNKNIVHMLVKALDRENFELLILVVTFLKKL 330
Cdd:pfam05804 241 KPIL---NSDYEKSLKKYKGLAKKQEQLLRVAFYLLLNLAEDVKLELKMRNKNIVKMLVKALDRDNIELLILVVSFLKKL 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823363439 331 SIFMENKNDMVEMDIVEKLVKMVPCEHEDLLNVTLRLLLNLSFDTGLRSKMVHVGLLPKLTALLGNENNKKVAICILYHI 410
Cdd:pfam05804 318 SIVGENKNEMGELNIVEKLPKLFPCTHEDLLNITLRLLLNLSFDTGLRRKMIAAGYLPKLVMLLNNDNHHGIAVCVLYHM 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823363439 411 SMDDCFKSMFAYTDCIPQLMKMLFECPDERVDLELISFCINLAANKRNVQLICEGNGLKMLMKRALKFKDPLLMKMIRNI 490
Cdd:pfam05804 398 SLDDKVKSMFTYTDCIPMAMKMIIENLNERVDLELIALCINLALNKRNAQLICEGNGLHSLMDRALKFQDPLLMKMIRNI 477
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823363439 491 SQHDGPTKSQFIEYVGDLAAQVSNDEEEEFVIECLGTLANLTLPELDWELVLKEYKLVPYLKDKLKPaGSAEDDLVLEVV 570
Cdd:pfam05804 478 SQHDGPLKLQFIDYVGDLARIITICDDEEFVVECLGILANLTIPDLDYEQILQEFQLVPWIKQKLLP-GAAEDDLVLEVV 556
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823363439 571 IMIGTVSMDDSCAALLAKSGIIPALIELLNAQQEDDEFVCQIIYVFYQMVFHQATRDVIIKETQAPAYLIDLMHDKNAEI 650
Cdd:pfam05804 557 VYLGTVACDDSCAALLAKSGIIISLIELLNAKQEDDEIVCQIIYVFYQMVFHEATREVIIKETQAPAYLIDLMHDKNEEI 636
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1823363439 651 RKVCDNTLDIIAEYDEEWAKKIQTEKFRWHNSQWLEMVESRQMDDSEQYL-YGDDPIEPYIHEGDILERPDL 721
Cdd:pfam05804 637 RKVCDNTLDIIAESDEEWAKKIKLEKFRWHNSQWLEMVESQQDDDNEQGLdYGDQEDEPYILESDILDRPDL 708
PRK05377 PRK05377
fructose-1,6-bisphosphate aldolase; Reviewed
561-608 5.18e-03

fructose-1,6-bisphosphate aldolase; Reviewed


Pssm-ID: 180045  Cd Length: 296  Bit Score: 39.86  E-value: 5.18e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1823363439 561 AEDDLVLEVVIMIGTVSMDDSCAALLAKSGIIP----ALIELLNAQQEDDEF 608
Cdd:PRK05377  228 IDHPRVLRVVALSGGYSRDEANELLARNHGLIAsfsrALTEGLSAQQSDEEF 279
 
Name Accession Description Interval E-value
KAP pfam05804
Kinesin-associated protein (KAP); This family consists of several eukaryotic ...
13-721 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: 1280.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823363439  13 VKGGNIDVHPSEKALIVHYEVEATILGELGDPMLGERKECQKIIRLKSLNANTDIGSLARKVVEECKLIHPSKLAEVEQL 92
Cdd:pfam05804   1 VKGGSIDVHPTEKALIVNYELEATILGEMGDPMLGERKECQKIIRLRSLNAKTDIAALAREVVEKCKLIHPSKLNEVEQL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823363439  93 LYYLQNRRDS--SAGKEKKEKTSKPKDPPPFEGTEIDEVANINDMDEYIELLYEDIPDKVRGSALILQLARNPDNLEELL 170
Cdd:pfam05804  81 LYYLQNRKDShtRSGARKHESVAKMKDPPPAEGPEADEVANINDIDEYIELLYEDLPEKVRGSALILQLARNPDNLEELE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823363439 171 INETALGALARVLREDWKQSIELATNIIYIFFCFSSFTQFHGIITHYKIGALCMNIIDHELKRHELWQEELAKKKKAVDE 250
Cdd:pfam05804 161 KNETCLGALARVLREDWKKSVELATNIIYIFFCFSSFSQFHPLIVHYKIGALCMDVIDHELKRHETWREELDKKKKMNEE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823363439 251 DPENqtlKKDYEKTYKKYKGLVVKQEQLLRVAIYLLLNLAEDTRIELKMRNKNIVHMLVKALDRENFELLILVVTFLKKL 330
Cdd:pfam05804 241 KPIL---NSDYEKSLKKYKGLAKKQEQLLRVAFYLLLNLAEDVKLELKMRNKNIVKMLVKALDRDNIELLILVVSFLKKL 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823363439 331 SIFMENKNDMVEMDIVEKLVKMVPCEHEDLLNVTLRLLLNLSFDTGLRSKMVHVGLLPKLTALLGNENNKKVAICILYHI 410
Cdd:pfam05804 318 SIVGENKNEMGELNIVEKLPKLFPCTHEDLLNITLRLLLNLSFDTGLRRKMIAAGYLPKLVMLLNNDNHHGIAVCVLYHM 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823363439 411 SMDDCFKSMFAYTDCIPQLMKMLFECPDERVDLELISFCINLAANKRNVQLICEGNGLKMLMKRALKFKDPLLMKMIRNI 490
Cdd:pfam05804 398 SLDDKVKSMFTYTDCIPMAMKMIIENLNERVDLELIALCINLALNKRNAQLICEGNGLHSLMDRALKFQDPLLMKMIRNI 477
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823363439 491 SQHDGPTKSQFIEYVGDLAAQVSNDEEEEFVIECLGTLANLTLPELDWELVLKEYKLVPYLKDKLKPaGSAEDDLVLEVV 570
Cdd:pfam05804 478 SQHDGPLKLQFIDYVGDLARIITICDDEEFVVECLGILANLTIPDLDYEQILQEFQLVPWIKQKLLP-GAAEDDLVLEVV 556
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823363439 571 IMIGTVSMDDSCAALLAKSGIIPALIELLNAQQEDDEFVCQIIYVFYQMVFHQATRDVIIKETQAPAYLIDLMHDKNAEI 650
Cdd:pfam05804 557 VYLGTVACDDSCAALLAKSGIIISLIELLNAKQEDDEIVCQIIYVFYQMVFHEATREVIIKETQAPAYLIDLMHDKNEEI 636
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1823363439 651 RKVCDNTLDIIAEYDEEWAKKIQTEKFRWHNSQWLEMVESRQMDDSEQYL-YGDDPIEPYIHEGDILERPDL 721
Cdd:pfam05804 637 RKVCDNTLDIIAESDEEWAKKIKLEKFRWHNSQWLEMVESQQDDDNEQGLdYGDQEDEPYILESDILDRPDL 708
PRK05377 PRK05377
fructose-1,6-bisphosphate aldolase; Reviewed
561-608 5.18e-03

fructose-1,6-bisphosphate aldolase; Reviewed


Pssm-ID: 180045  Cd Length: 296  Bit Score: 39.86  E-value: 5.18e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1823363439 561 AEDDLVLEVVIMIGTVSMDDSCAALLAKSGIIP----ALIELLNAQQEDDEF 608
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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