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Conserved domains on  [gi|81884563|sp|Q6AYB8|]
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RecName: Full=Golgin-45; AltName: Full=Basic leucine zipper nuclear factor 1

Protein Classification

DASH complex subunit HSK3 family protein( domain architecture ID 10548802)

DASH complex subunit HSK3 is a component of the DASH complex, a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation

Gene Ontology:  GO:0051301|GO:0045787

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DASH_Hsk3 pfam08227
DASH complex subunit Hsk3 like; The DASH complex is a ~10 subunit microtubule-binding complex ...
 184-229 1.78e-06

DASH complex subunit Hsk3 like; The DASH complex is a ~10 subunit microtubule-binding complex that is transferred to the kinetochore prior to mitosis. In Saccharomyces cerevisiae DASH forms both rings and spiral structures on microtubules in vitro. This family also includes several higher eukaryotic proteins. However, other DASH subunits do not appear to be conserved in higher eukaryotes.


:

Pssm-ID: 429874 [Multi-domain]  Cd Length: 45  Bit Score: 44.48  E-value: 1.78e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 81884563   184 AREKNQLILENEALGRNTAQLSEQLERMSIQCDVwrSKFLASRVMA 229
Cdd:pfam08227   1 QRQYSHLASQLAQLQANLADTEELLRMTSEQANS--IRKLGKYHAS 44
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 109-279 1.75e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 1.75e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884563 109 REELHNQSEVVTDPRKELSEVKKVLEKLKNSERRLLQDKEGLSNQLRVQTEVNRELKKLLVASVGDDpqyhfERLAREKN 188
Cdd:COG1196 273 RLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL-----EELEEELE 347

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884563 189 QLILENEALGRNTAQLSEQLERMSIQCDVWRSKFLASRVMADELTNFRVVLQHQNRDAQSAIQDLLSEREQFRQEMISTQ 268
Cdd:COG1196 348 EAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE 427

                       170
                ....*....|.
gi 81884563 269 KFLEELLVSLQ 279
Cdd:COG1196 428 EALAELEEEEE 438
 
Name Accession Description Interval E-value
DASH_Hsk3 pfam08227
DASH complex subunit Hsk3 like; The DASH complex is a ~10 subunit microtubule-binding complex ...
 184-229 1.78e-06

DASH complex subunit Hsk3 like; The DASH complex is a ~10 subunit microtubule-binding complex that is transferred to the kinetochore prior to mitosis. In Saccharomyces cerevisiae DASH forms both rings and spiral structures on microtubules in vitro. This family also includes several higher eukaryotic proteins. However, other DASH subunits do not appear to be conserved in higher eukaryotes.


Pssm-ID: 429874 [Multi-domain]  Cd Length: 45  Bit Score: 44.48  E-value: 1.78e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 81884563   184 AREKNQLILENEALGRNTAQLSEQLERMSIQCDVwrSKFLASRVMA 229
Cdd:pfam08227   1 QRQYSHLASQLAQLQANLADTEELLRMTSEQANS--IRKLGKYHAS 44
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 109-279 1.75e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 1.75e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884563 109 REELHNQSEVVTDPRKELSEVKKVLEKLKNSERRLLQDKEGLSNQLRVQTEVNRELKKLLVASVGDDpqyhfERLAREKN 188
Cdd:COG1196 273 RLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL-----EELEEELE 347

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884563 189 QLILENEALGRNTAQLSEQLERMSIQCDVWRSKFLASRVMADELTNFRVVLQHQNRDAQSAIQDLLSEREQFRQEMISTQ 268
Cdd:COG1196 348 EAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE 427

                       170
                ....*....|.
gi 81884563 269 KFLEELLVSLQ 279
Cdd:COG1196 428 EALAELEEEEE 438
 
Name Accession Description Interval E-value
DASH_Hsk3 pfam08227
DASH complex subunit Hsk3 like; The DASH complex is a ~10 subunit microtubule-binding complex ...
 184-229 1.78e-06

DASH complex subunit Hsk3 like; The DASH complex is a ~10 subunit microtubule-binding complex that is transferred to the kinetochore prior to mitosis. In Saccharomyces cerevisiae DASH forms both rings and spiral structures on microtubules in vitro. This family also includes several higher eukaryotic proteins. However, other DASH subunits do not appear to be conserved in higher eukaryotes.


Pssm-ID: 429874 [Multi-domain]  Cd Length: 45  Bit Score: 44.48  E-value: 1.78e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 81884563   184 AREKNQLILENEALGRNTAQLSEQLERMSIQCDVwrSKFLASRVMA 229
Cdd:pfam08227   1 QRQYSHLASQLAQLQANLADTEELLRMTSEQANS--IRKLGKYHAS 44
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 109-279 1.75e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 1.75e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884563 109 REELHNQSEVVTDPRKELSEVKKVLEKLKNSERRLLQDKEGLSNQLRVQTEVNRELKKLLVASVGDDpqyhfERLAREKN 188
Cdd:COG1196 273 RLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL-----EELEEELE 347

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884563 189 QLILENEALGRNTAQLSEQLERMSIQCDVWRSKFLASRVMADELTNFRVVLQHQNRDAQSAIQDLLSEREQFRQEMISTQ 268
Cdd:COG1196 348 EAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE 427

                       170
                ....*....|.
gi 81884563 269 KFLEELLVSLQ 279
Cdd:COG1196 428 EALAELEEEEE 438
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
123-263 3.36e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.90  E-value: 3.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884563  123 RKELSEVKKVLEKLKNSERRLLQDKEGLSNQLRVQTEVNRELKKLLVASVGDDpqyhFERLAREKNQLILENEALGRNTA 202
Cdd:COG4913  287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDR----LEQLEREIERLERELEERERRRA 362

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 81884563  203 QLSEQLERMSIQCDVWRSKFLASRVMADELTNFRVVLQHQNRDAQ----SAIQDLLSEREQFRQE 263
Cdd:COG4913  363 RLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALaeaeAALRDLRRELRELEAE 427
 
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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