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Conserved domains on  [gi|299522838|ref|NP_001177382|]
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dynactin subunit 2 isoform 2 [Mus musculus]

Protein Classification

dynactin subunit 2( domain architecture ID 12059144)

dynactin subunit 2 is a component of dynactin, a multiprotein complex associated with dynein, that modulates cytoplasmic dynein binding to an organelle, and plays a role in prometaphase chromosome alignment and spindle organization during mitosis

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Dynamitin pfam04912
Dynamitin; Dynamitin is a subunit of the microtubule-dependent motor complex and in implicated ...
16-402 1.01e-154

Dynamitin; Dynamitin is a subunit of the microtubule-dependent motor complex and in implicated in cell adhesion by binding to macrophage-enriched myristoylated alanine-rice C kinase substrate (MacMARCKS).


:

Pssm-ID: 461477 [Multi-domain]  Cd Length: 390  Bit Score: 442.16  E-value: 1.01e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299522838   16 EPDVYETSDLPEDDQAEFDA-----ELEELSSTSVEHIIVNPNAAYDKFKDKRVGTKGLDFSDRIGKTKRTGYE---SGD 87
Cdd:pfam04912   1 QPDVYETPDLPEDDQTDDEStahseSEEELENEDIERSSLNPNEARNKFKGKRLDAKGVDFSDRISKKKRTGYRtssSGE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299522838   88 YEMLGEGlGVKETPQQKYQRLLHEVQELTTEVEKIKTTVKESateEKLTPVVLAKQLAALKQQLVASHLEKLLGPDAAIN 167
Cdd:pfam04912  81 YELAGEG-EEKETPEQKLQRLQREVEELEEEVEKRKAAAKES---EKADPVELAAQLASLQKQLDELKLEELLGPDVAIG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299522838  168 LADPDGALAKRLLLQLEATKSSKGSSGGKATAGAPPDSSLVTYELHSRPEQDKFSQAAKVAELEKRLTELEATVRCDQDA 247
Cdd:pfam04912 157 LTDPQGALSKRLLSQLEAFKQTSAPSGKKEPSASEPPSNHVTYELYYRPEQAKSQQLAKIAELEKRLAELEKLVGIDSDL 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299522838  248 QNPLSAGLQGACLMETVELLQAKVSALDLAVLDQVEARLQSVLGKVNEIAKHKAsVEDADTQNKVHQLYETIQRWSPVAS 327
Cdd:pfam04912 237 LDELSANLGPAPLLETLSRLQAKLSLLDPAHLDAIERRLKSLLAEMDELAEKRE-KADATQEAKINELYELLPRWDPLSP 315
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 299522838  328 TLPELVQRLVTIKQLHEQAMQFGQLLTHLDTTQQMMASSLKDNTALLTQVQTTMRENLATVEGNFASIDARMKRL 402
Cdd:pfam04912 316 ILPPVLDRLRTLRALHEQAAEFSQTLTELETTQSEIAEELKSNKELLEKVEESFKENLTTVKSNIESLEERVKKL 390
 
Name Accession Description Interval E-value
Dynamitin pfam04912
Dynamitin; Dynamitin is a subunit of the microtubule-dependent motor complex and in implicated ...
16-402 1.01e-154

Dynamitin; Dynamitin is a subunit of the microtubule-dependent motor complex and in implicated in cell adhesion by binding to macrophage-enriched myristoylated alanine-rice C kinase substrate (MacMARCKS).


Pssm-ID: 461477 [Multi-domain]  Cd Length: 390  Bit Score: 442.16  E-value: 1.01e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299522838   16 EPDVYETSDLPEDDQAEFDA-----ELEELSSTSVEHIIVNPNAAYDKFKDKRVGTKGLDFSDRIGKTKRTGYE---SGD 87
Cdd:pfam04912   1 QPDVYETPDLPEDDQTDDEStahseSEEELENEDIERSSLNPNEARNKFKGKRLDAKGVDFSDRISKKKRTGYRtssSGE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299522838   88 YEMLGEGlGVKETPQQKYQRLLHEVQELTTEVEKIKTTVKESateEKLTPVVLAKQLAALKQQLVASHLEKLLGPDAAIN 167
Cdd:pfam04912  81 YELAGEG-EEKETPEQKLQRLQREVEELEEEVEKRKAAAKES---EKADPVELAAQLASLQKQLDELKLEELLGPDVAIG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299522838  168 LADPDGALAKRLLLQLEATKSSKGSSGGKATAGAPPDSSLVTYELHSRPEQDKFSQAAKVAELEKRLTELEATVRCDQDA 247
Cdd:pfam04912 157 LTDPQGALSKRLLSQLEAFKQTSAPSGKKEPSASEPPSNHVTYELYYRPEQAKSQQLAKIAELEKRLAELEKLVGIDSDL 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299522838  248 QNPLSAGLQGACLMETVELLQAKVSALDLAVLDQVEARLQSVLGKVNEIAKHKAsVEDADTQNKVHQLYETIQRWSPVAS 327
Cdd:pfam04912 237 LDELSANLGPAPLLETLSRLQAKLSLLDPAHLDAIERRLKSLLAEMDELAEKRE-KADATQEAKINELYELLPRWDPLSP 315
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 299522838  328 TLPELVQRLVTIKQLHEQAMQFGQLLTHLDTTQQMMASSLKDNTALLTQVQTTMRENLATVEGNFASIDARMKRL 402
Cdd:pfam04912 316 ILPPVLDRLRTLRALHEQAAEFSQTLTELETTQSEIAEELKSNKELLEKVEESFKENLTTVKSNIESLEERVKKL 390
 
Name Accession Description Interval E-value
Dynamitin pfam04912
Dynamitin; Dynamitin is a subunit of the microtubule-dependent motor complex and in implicated ...
16-402 1.01e-154

Dynamitin; Dynamitin is a subunit of the microtubule-dependent motor complex and in implicated in cell adhesion by binding to macrophage-enriched myristoylated alanine-rice C kinase substrate (MacMARCKS).


Pssm-ID: 461477 [Multi-domain]  Cd Length: 390  Bit Score: 442.16  E-value: 1.01e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299522838   16 EPDVYETSDLPEDDQAEFDA-----ELEELSSTSVEHIIVNPNAAYDKFKDKRVGTKGLDFSDRIGKTKRTGYE---SGD 87
Cdd:pfam04912   1 QPDVYETPDLPEDDQTDDEStahseSEEELENEDIERSSLNPNEARNKFKGKRLDAKGVDFSDRISKKKRTGYRtssSGE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299522838   88 YEMLGEGlGVKETPQQKYQRLLHEVQELTTEVEKIKTTVKESateEKLTPVVLAKQLAALKQQLVASHLEKLLGPDAAIN 167
Cdd:pfam04912  81 YELAGEG-EEKETPEQKLQRLQREVEELEEEVEKRKAAAKES---EKADPVELAAQLASLQKQLDELKLEELLGPDVAIG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299522838  168 LADPDGALAKRLLLQLEATKSSKGSSGGKATAGAPPDSSLVTYELHSRPEQDKFSQAAKVAELEKRLTELEATVRCDQDA 247
Cdd:pfam04912 157 LTDPQGALSKRLLSQLEAFKQTSAPSGKKEPSASEPPSNHVTYELYYRPEQAKSQQLAKIAELEKRLAELEKLVGIDSDL 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299522838  248 QNPLSAGLQGACLMETVELLQAKVSALDLAVLDQVEARLQSVLGKVNEIAKHKAsVEDADTQNKVHQLYETIQRWSPVAS 327
Cdd:pfam04912 237 LDELSANLGPAPLLETLSRLQAKLSLLDPAHLDAIERRLKSLLAEMDELAEKRE-KADATQEAKINELYELLPRWDPLSP 315
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 299522838  328 TLPELVQRLVTIKQLHEQAMQFGQLLTHLDTTQQMMASSLKDNTALLTQVQTTMRENLATVEGNFASIDARMKRL 402
Cdd:pfam04912 316 ILPPVLDRLRTLRALHEQAAEFSQTLTELETTQSEIAEELKSNKELLEKVEESFKENLTTVKSNIESLEERVKKL 390
 
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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