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Conserved domains on  [gi|109288014|ref|NP_001035886|]
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kinetochore-associated protein 1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Rod_C pfam10493
Rough deal protein C-terminal region; Rod, the Rough deal protein, displays a dynamic ...
1579-2128 0e+00

Rough deal protein C-terminal region; Rod, the Rough deal protein, displays a dynamic intracellular staining pattern, localising first to kinetochores in pro-metaphase, but moving to kinetochore microtubules at metaphase. Early in anaphase the protein is once again restricted to the kinetochores, where it persists until the end of telophase. This behaviour is in all respects similar to that described for ZW10, and indeed the two proteins function together, localization of each depending upon the other. These two proteins are found at the kinetochore in complex with a third, Zwilch, in both flies and humans. The C-terminus is the most conserved part of the protein. During pro-metaphase, the ZW10-Rod complex, dynein/dynactin, and Mad2 all accumulate on unattached kinetochores; microtubule capture leads to Mad2 depletion as it is carried off by dynein/dynactin; ZW10-Rod complex accumulation continues, replenishing kinetochore dynein. The continuing recruitment of the ZW10-Rod complex during metaphase may serve to maintain adequate dynein/dynactin complex on kinetochores for assisting chromatid movement during anaphase. The ZW10-Rod complex acts as a bridge whose association with Zwint-1 links Mad1 and Mad2, components that are directly responsible for generating the diffusible 'wait anaphase' signal, to a structural, inner kinetochore complex containing Mis12 and KNL-1AF15q14, the last of which has been proved to be essential for kinetochore assembly in C. elegans. Removal of ZW10 or Rod inactivates the mitotic checkpoint.


:

Pssm-ID: 463114  Cd Length: 551  Bit Score: 922.15  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109288014  1579 MITLPPAAHTRLPFHLILfgTAQNFWKILSSELSEESLPTLLLIAKLMKFSLDTLYVSTAKHLFEKNLKPKLLKSAQARS 1658
Cdd:pfam10493    1 GIVLPPIAQTRLPFHLIF--TEQPFWKILSAELSEESFPTLLLISKLMKVSLDTLYMSAANDVFEKSLKPNSLKEYKSKN 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109288014  1659 STLMSKEVDKLMQTLESYLLSIVNPEWAVAIAISLTQEVPEGPFKMSSLKFCLYLAERWLQNIPPQDETCEKAKALQKKL 1738
Cdd:pfam10493   79 SSEANKENNKFLQTILSYLLSIKNPEWAFAIAYKIAQELPEGPDKVEALYFCLKLAEKWLKNLAPDDEAREKAEALLKKL 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109288014  1739 CLQVRLSGTEAVLIAHKLNDQEYLRVIGKPAHLIVSLYEHPSISERLCTTSGKDYPDIHTAAKEIAEVNEVNLEKIWDML 1818
Cdd:pfam10493  159 KRQYQRSKTENLLIAHGLNDEELLKLVGKPAELIVSLYEHSSIEQRYKNPGGRDYPDIHAAVKEIAEINELDLEKIQDML 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109288014  1819 LEKWLCPSTVP--SEKASEFF-ELEEDEVLHRVVYLLQARPVDYCSRMLFVFATSATSTLGMRQLTFAHKARALQCLLYL 1895
Cdd:pfam10493  239 LEKWLCPTMEPtdGTKLEETFlDIQEDEDLRRVVYLLQSWPIDYSVRMLFAIATSETSPLGVNQLTFAHRLRALQCLLKL 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109288014  1896 ADKETIESLFKKPIKEMKSYLKCITFLASFETLNIPITYELFCNSPKEGMIKGLWKNHSHEPMAVRLVAELCLEYKIYDL 1975
Cdd:pfam10493  319 ADGETIESLFKKPIEQVKYYLKCVIFLASFEYLNIPYTYESFHSSPKEGMIKGLWKNHSHEPMAVRLVAELCLEYQVYDP 398
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109288014  1976 QLWNGLLQKLLGFNMIPYLRKVLSCISSIHSLWQVPYFSKAWQRVIQIPLLSASCPLRPSQLADCCDSLVAILECPVSDD 2055
Cdd:pfam10493  399 QLWNGLLQKLLGFNMISYLRKVLDAISSVHSLWQIPGFSRAWQSVILAPLLSASCPLSPDQLEDLYESLVLLLKCPVSDD 478
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 109288014  2056 LDMMGVAKQYVQLDLPAFALTCLTLMPHSEKRHQQIKNFLNSCDARIILQQIEEHMNTGQLAGFSHQIGSLVL 2128
Cdd:pfam10493  479 LDLIGIAKQYVQLDLPAFALACLLLIPQSEKRRQQIKKFLSSCNPENLLQQIDELMNTGELAGFASQIRKLVL 551
Rod_C super family cl20400
Rough deal protein C-terminal region; Rod, the Rough deal protein, displays a dynamic ...
487-744 4.14e-35

Rough deal protein C-terminal region; Rod, the Rough deal protein, displays a dynamic intracellular staining pattern, localising first to kinetochores in pro-metaphase, but moving to kinetochore microtubules at metaphase. Early in anaphase the protein is once again restricted to the kinetochores, where it persists until the end of telophase. This behaviour is in all respects similar to that described for ZW10, and indeed the two proteins function together, localization of each depending upon the other. These two proteins are found at the kinetochore in complex with a third, Zwilch, in both flies and humans. The C-terminus is the most conserved part of the protein. During pro-metaphase, the ZW10-Rod complex, dynein/dynactin, and Mad2 all accumulate on unattached kinetochores; microtubule capture leads to Mad2 depletion as it is carried off by dynein/dynactin; ZW10-Rod complex accumulation continues, replenishing kinetochore dynein. The continuing recruitment of the ZW10-Rod complex during metaphase may serve to maintain adequate dynein/dynactin complex on kinetochores for assisting chromatid movement during anaphase. The ZW10-Rod complex acts as a bridge whose association with Zwint-1 links Mad1 and Mad2, components that are directly responsible for generating the diffusible 'wait anaphase' signal, to a structural, inner kinetochore complex containing Mis12 and KNL-1AF15q14, the last of which has been proved to be essential for kinetochore assembly in C. elegans. Removal of ZW10 or Rod inactivates the mitotic checkpoint.


The actual alignment was detected with superfamily member pfam10493:

Pssm-ID: 463114  Cd Length: 551  Bit Score: 143.28  E-value: 4.14e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109288014   487 TQEMLSYAKTRLMKKedraLPASSDAFMEVLKAHAKLTTFYGAFGPEKFSGSSWIEFLNNEDDlrDVFLQLSEGNFACAQ 566
Cdd:pfam10493    1 GIVLPPIAQTRLPFH----LIFTEQPFWKILSAELSEESFPTLLLISKLMKVSLDTLYMSAAN--DVFEKSLKPNSLKEY 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109288014   567 YLWLRHRADFESKFDVKMLENLLNSISTQFPLENLCSWFKNEVIPFVRRI--VPEGQNILAKWLEQASRNLELTDKAnwp 644
Cdd:pfam10493   75 KSKNSSEANKENNKFLQTILSYLLSIKNPEWAFAIAYKIAQELPEGPDKVeaLYFCLKLAEKWLKNLAPDDEAREKA--- 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109288014   645 ENGLQLAEVFFTAEKTDRFGFASSWHwislDYQNTEEVRQLRTLVSKLRELIILHRKYNCKLAlSDFEKENATTVVFRMF 724
Cdd:pfam10493  152 EALLKKLKRQYQRSKTENLLIAHGLN----DEELLKLVGKPAELIVSLYEHSSIEQRYKNPGG-RDYPDIHAAVKEIAEI 226
                          250       260
                   ....*....|....*....|
gi 109288014   725 DRVSAPELIPSVLEKSVRVY 744
Cdd:pfam10493  227 NELDLEKIQDMLLEKWLCPT 246
 
Name Accession Description Interval E-value
Rod_C pfam10493
Rough deal protein C-terminal region; Rod, the Rough deal protein, displays a dynamic ...
1579-2128 0e+00

Rough deal protein C-terminal region; Rod, the Rough deal protein, displays a dynamic intracellular staining pattern, localising first to kinetochores in pro-metaphase, but moving to kinetochore microtubules at metaphase. Early in anaphase the protein is once again restricted to the kinetochores, where it persists until the end of telophase. This behaviour is in all respects similar to that described for ZW10, and indeed the two proteins function together, localization of each depending upon the other. These two proteins are found at the kinetochore in complex with a third, Zwilch, in both flies and humans. The C-terminus is the most conserved part of the protein. During pro-metaphase, the ZW10-Rod complex, dynein/dynactin, and Mad2 all accumulate on unattached kinetochores; microtubule capture leads to Mad2 depletion as it is carried off by dynein/dynactin; ZW10-Rod complex accumulation continues, replenishing kinetochore dynein. The continuing recruitment of the ZW10-Rod complex during metaphase may serve to maintain adequate dynein/dynactin complex on kinetochores for assisting chromatid movement during anaphase. The ZW10-Rod complex acts as a bridge whose association with Zwint-1 links Mad1 and Mad2, components that are directly responsible for generating the diffusible 'wait anaphase' signal, to a structural, inner kinetochore complex containing Mis12 and KNL-1AF15q14, the last of which has been proved to be essential for kinetochore assembly in C. elegans. Removal of ZW10 or Rod inactivates the mitotic checkpoint.


Pssm-ID: 463114  Cd Length: 551  Bit Score: 922.15  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109288014  1579 MITLPPAAHTRLPFHLILfgTAQNFWKILSSELSEESLPTLLLIAKLMKFSLDTLYVSTAKHLFEKNLKPKLLKSAQARS 1658
Cdd:pfam10493    1 GIVLPPIAQTRLPFHLIF--TEQPFWKILSAELSEESFPTLLLISKLMKVSLDTLYMSAANDVFEKSLKPNSLKEYKSKN 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109288014  1659 STLMSKEVDKLMQTLESYLLSIVNPEWAVAIAISLTQEVPEGPFKMSSLKFCLYLAERWLQNIPPQDETCEKAKALQKKL 1738
Cdd:pfam10493   79 SSEANKENNKFLQTILSYLLSIKNPEWAFAIAYKIAQELPEGPDKVEALYFCLKLAEKWLKNLAPDDEAREKAEALLKKL 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109288014  1739 CLQVRLSGTEAVLIAHKLNDQEYLRVIGKPAHLIVSLYEHPSISERLCTTSGKDYPDIHTAAKEIAEVNEVNLEKIWDML 1818
Cdd:pfam10493  159 KRQYQRSKTENLLIAHGLNDEELLKLVGKPAELIVSLYEHSSIEQRYKNPGGRDYPDIHAAVKEIAEINELDLEKIQDML 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109288014  1819 LEKWLCPSTVP--SEKASEFF-ELEEDEVLHRVVYLLQARPVDYCSRMLFVFATSATSTLGMRQLTFAHKARALQCLLYL 1895
Cdd:pfam10493  239 LEKWLCPTMEPtdGTKLEETFlDIQEDEDLRRVVYLLQSWPIDYSVRMLFAIATSETSPLGVNQLTFAHRLRALQCLLKL 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109288014  1896 ADKETIESLFKKPIKEMKSYLKCITFLASFETLNIPITYELFCNSPKEGMIKGLWKNHSHEPMAVRLVAELCLEYKIYDL 1975
Cdd:pfam10493  319 ADGETIESLFKKPIEQVKYYLKCVIFLASFEYLNIPYTYESFHSSPKEGMIKGLWKNHSHEPMAVRLVAELCLEYQVYDP 398
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109288014  1976 QLWNGLLQKLLGFNMIPYLRKVLSCISSIHSLWQVPYFSKAWQRVIQIPLLSASCPLRPSQLADCCDSLVAILECPVSDD 2055
Cdd:pfam10493  399 QLWNGLLQKLLGFNMISYLRKVLDAISSVHSLWQIPGFSRAWQSVILAPLLSASCPLSPDQLEDLYESLVLLLKCPVSDD 478
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 109288014  2056 LDMMGVAKQYVQLDLPAFALTCLTLMPHSEKRHQQIKNFLNSCDARIILQQIEEHMNTGQLAGFSHQIGSLVL 2128
Cdd:pfam10493  479 LDLIGIAKQYVQLDLPAFALACLLLIPQSEKRRQQIKKFLSSCNPENLLQQIDELMNTGELAGFASQIRKLVL 551
Rod_C pfam10493
Rough deal protein C-terminal region; Rod, the Rough deal protein, displays a dynamic ...
487-744 4.14e-35

Rough deal protein C-terminal region; Rod, the Rough deal protein, displays a dynamic intracellular staining pattern, localising first to kinetochores in pro-metaphase, but moving to kinetochore microtubules at metaphase. Early in anaphase the protein is once again restricted to the kinetochores, where it persists until the end of telophase. This behaviour is in all respects similar to that described for ZW10, and indeed the two proteins function together, localization of each depending upon the other. These two proteins are found at the kinetochore in complex with a third, Zwilch, in both flies and humans. The C-terminus is the most conserved part of the protein. During pro-metaphase, the ZW10-Rod complex, dynein/dynactin, and Mad2 all accumulate on unattached kinetochores; microtubule capture leads to Mad2 depletion as it is carried off by dynein/dynactin; ZW10-Rod complex accumulation continues, replenishing kinetochore dynein. The continuing recruitment of the ZW10-Rod complex during metaphase may serve to maintain adequate dynein/dynactin complex on kinetochores for assisting chromatid movement during anaphase. The ZW10-Rod complex acts as a bridge whose association with Zwint-1 links Mad1 and Mad2, components that are directly responsible for generating the diffusible 'wait anaphase' signal, to a structural, inner kinetochore complex containing Mis12 and KNL-1AF15q14, the last of which has been proved to be essential for kinetochore assembly in C. elegans. Removal of ZW10 or Rod inactivates the mitotic checkpoint.


Pssm-ID: 463114  Cd Length: 551  Bit Score: 143.28  E-value: 4.14e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109288014   487 TQEMLSYAKTRLMKKedraLPASSDAFMEVLKAHAKLTTFYGAFGPEKFSGSSWIEFLNNEDDlrDVFLQLSEGNFACAQ 566
Cdd:pfam10493    1 GIVLPPIAQTRLPFH----LIFTEQPFWKILSAELSEESFPTLLLISKLMKVSLDTLYMSAAN--DVFEKSLKPNSLKEY 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109288014   567 YLWLRHRADFESKFDVKMLENLLNSISTQFPLENLCSWFKNEVIPFVRRI--VPEGQNILAKWLEQASRNLELTDKAnwp 644
Cdd:pfam10493   75 KSKNSSEANKENNKFLQTILSYLLSIKNPEWAFAIAYKIAQELPEGPDKVeaLYFCLKLAEKWLKNLAPDDEAREKA--- 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109288014   645 ENGLQLAEVFFTAEKTDRFGFASSWHwislDYQNTEEVRQLRTLVSKLRELIILHRKYNCKLAlSDFEKENATTVVFRMF 724
Cdd:pfam10493  152 EALLKKLKRQYQRSKTENLLIAHGLN----DEELLKLVGKPAELIVSLYEHSSIEQRYKNPGG-RDYPDIHAAVKEIAEI 226
                          250       260
                   ....*....|....*....|
gi 109288014   725 DRVSAPELIPSVLEKSVRVY 744
Cdd:pfam10493  227 NELDLEKIQDMLLEKWLCPT 246
 
Name Accession Description Interval E-value
Rod_C pfam10493
Rough deal protein C-terminal region; Rod, the Rough deal protein, displays a dynamic ...
1579-2128 0e+00

Rough deal protein C-terminal region; Rod, the Rough deal protein, displays a dynamic intracellular staining pattern, localising first to kinetochores in pro-metaphase, but moving to kinetochore microtubules at metaphase. Early in anaphase the protein is once again restricted to the kinetochores, where it persists until the end of telophase. This behaviour is in all respects similar to that described for ZW10, and indeed the two proteins function together, localization of each depending upon the other. These two proteins are found at the kinetochore in complex with a third, Zwilch, in both flies and humans. The C-terminus is the most conserved part of the protein. During pro-metaphase, the ZW10-Rod complex, dynein/dynactin, and Mad2 all accumulate on unattached kinetochores; microtubule capture leads to Mad2 depletion as it is carried off by dynein/dynactin; ZW10-Rod complex accumulation continues, replenishing kinetochore dynein. The continuing recruitment of the ZW10-Rod complex during metaphase may serve to maintain adequate dynein/dynactin complex on kinetochores for assisting chromatid movement during anaphase. The ZW10-Rod complex acts as a bridge whose association with Zwint-1 links Mad1 and Mad2, components that are directly responsible for generating the diffusible 'wait anaphase' signal, to a structural, inner kinetochore complex containing Mis12 and KNL-1AF15q14, the last of which has been proved to be essential for kinetochore assembly in C. elegans. Removal of ZW10 or Rod inactivates the mitotic checkpoint.


Pssm-ID: 463114  Cd Length: 551  Bit Score: 922.15  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109288014  1579 MITLPPAAHTRLPFHLILfgTAQNFWKILSSELSEESLPTLLLIAKLMKFSLDTLYVSTAKHLFEKNLKPKLLKSAQARS 1658
Cdd:pfam10493    1 GIVLPPIAQTRLPFHLIF--TEQPFWKILSAELSEESFPTLLLISKLMKVSLDTLYMSAANDVFEKSLKPNSLKEYKSKN 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109288014  1659 STLMSKEVDKLMQTLESYLLSIVNPEWAVAIAISLTQEVPEGPFKMSSLKFCLYLAERWLQNIPPQDETCEKAKALQKKL 1738
Cdd:pfam10493   79 SSEANKENNKFLQTILSYLLSIKNPEWAFAIAYKIAQELPEGPDKVEALYFCLKLAEKWLKNLAPDDEAREKAEALLKKL 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109288014  1739 CLQVRLSGTEAVLIAHKLNDQEYLRVIGKPAHLIVSLYEHPSISERLCTTSGKDYPDIHTAAKEIAEVNEVNLEKIWDML 1818
Cdd:pfam10493  159 KRQYQRSKTENLLIAHGLNDEELLKLVGKPAELIVSLYEHSSIEQRYKNPGGRDYPDIHAAVKEIAEINELDLEKIQDML 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109288014  1819 LEKWLCPSTVP--SEKASEFF-ELEEDEVLHRVVYLLQARPVDYCSRMLFVFATSATSTLGMRQLTFAHKARALQCLLYL 1895
Cdd:pfam10493  239 LEKWLCPTMEPtdGTKLEETFlDIQEDEDLRRVVYLLQSWPIDYSVRMLFAIATSETSPLGVNQLTFAHRLRALQCLLKL 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109288014  1896 ADKETIESLFKKPIKEMKSYLKCITFLASFETLNIPITYELFCNSPKEGMIKGLWKNHSHEPMAVRLVAELCLEYKIYDL 1975
Cdd:pfam10493  319 ADGETIESLFKKPIEQVKYYLKCVIFLASFEYLNIPYTYESFHSSPKEGMIKGLWKNHSHEPMAVRLVAELCLEYQVYDP 398
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109288014  1976 QLWNGLLQKLLGFNMIPYLRKVLSCISSIHSLWQVPYFSKAWQRVIQIPLLSASCPLRPSQLADCCDSLVAILECPVSDD 2055
Cdd:pfam10493  399 QLWNGLLQKLLGFNMISYLRKVLDAISSVHSLWQIPGFSRAWQSVILAPLLSASCPLSPDQLEDLYESLVLLLKCPVSDD 478
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 109288014  2056 LDMMGVAKQYVQLDLPAFALTCLTLMPHSEKRHQQIKNFLNSCDARIILQQIEEHMNTGQLAGFSHQIGSLVL 2128
Cdd:pfam10493  479 LDLIGIAKQYVQLDLPAFALACLLLIPQSEKRRQQIKKFLSSCNPENLLQQIDELMNTGELAGFASQIRKLVL 551
Rod_C pfam10493
Rough deal protein C-terminal region; Rod, the Rough deal protein, displays a dynamic ...
487-744 4.14e-35

Rough deal protein C-terminal region; Rod, the Rough deal protein, displays a dynamic intracellular staining pattern, localising first to kinetochores in pro-metaphase, but moving to kinetochore microtubules at metaphase. Early in anaphase the protein is once again restricted to the kinetochores, where it persists until the end of telophase. This behaviour is in all respects similar to that described for ZW10, and indeed the two proteins function together, localization of each depending upon the other. These two proteins are found at the kinetochore in complex with a third, Zwilch, in both flies and humans. The C-terminus is the most conserved part of the protein. During pro-metaphase, the ZW10-Rod complex, dynein/dynactin, and Mad2 all accumulate on unattached kinetochores; microtubule capture leads to Mad2 depletion as it is carried off by dynein/dynactin; ZW10-Rod complex accumulation continues, replenishing kinetochore dynein. The continuing recruitment of the ZW10-Rod complex during metaphase may serve to maintain adequate dynein/dynactin complex on kinetochores for assisting chromatid movement during anaphase. The ZW10-Rod complex acts as a bridge whose association with Zwint-1 links Mad1 and Mad2, components that are directly responsible for generating the diffusible 'wait anaphase' signal, to a structural, inner kinetochore complex containing Mis12 and KNL-1AF15q14, the last of which has been proved to be essential for kinetochore assembly in C. elegans. Removal of ZW10 or Rod inactivates the mitotic checkpoint.


Pssm-ID: 463114  Cd Length: 551  Bit Score: 143.28  E-value: 4.14e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109288014   487 TQEMLSYAKTRLMKKedraLPASSDAFMEVLKAHAKLTTFYGAFGPEKFSGSSWIEFLNNEDDlrDVFLQLSEGNFACAQ 566
Cdd:pfam10493    1 GIVLPPIAQTRLPFH----LIFTEQPFWKILSAELSEESFPTLLLISKLMKVSLDTLYMSAAN--DVFEKSLKPNSLKEY 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109288014   567 YLWLRHRADFESKFDVKMLENLLNSISTQFPLENLCSWFKNEVIPFVRRI--VPEGQNILAKWLEQASRNLELTDKAnwp 644
Cdd:pfam10493   75 KSKNSSEANKENNKFLQTILSYLLSIKNPEWAFAIAYKIAQELPEGPDKVeaLYFCLKLAEKWLKNLAPDDEAREKA--- 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109288014   645 ENGLQLAEVFFTAEKTDRFGFASSWHwislDYQNTEEVRQLRTLVSKLRELIILHRKYNCKLAlSDFEKENATTVVFRMF 724
Cdd:pfam10493  152 EALLKKLKRQYQRSKTENLLIAHGLN----DEELLKLVGKPAELIVSLYEHSSIEQRYKNPGG-RDYPDIHAAVKEIAEI 226
                          250       260
                   ....*....|....*....|
gi 109288014   725 DRVSAPELIPSVLEKSVRVY 744
Cdd:pfam10493  227 NELDLEKIQDMLLEKWLCPT 246
 
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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