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Conserved domains on  [gi|1034582450|ref|XP_016875744|]
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kinetochore-associated protein 1 isoform X5 [Homo sapiens]

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 ...
1429-1977 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: 936.02  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034582450 1429 ITLPSAAQTRLPFHLIFfgTAQNFWKILSTELSEESFPTLLLISKLMKFSLDTLYVSTAKHVFEKKLKPKLLKLTQAKSS 1508
Cdd:pfam10493    2 IVLPPIAQTRLPFHLIF--TEQPFWKILSAELSEESFPTLLLISKLMKVSLDTLYMSAANDVFEKSLKPNSLKEYKSKNS 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034582450 1509 TLINKEITKITQTIESCLLSIVNPEWAVAIAISLAQDIPEGSFKISALKFCLYLAERWLQNIPSQDEKREKAEALLKKLH 1588
Cdd:pfam10493   80 SEANKENNKFLQTILSYLLSIKNPEWAFAIAYKIAQELPEGPDKVEALYFCLKLAEKWLKNLAPDDEAREKAEALLKKLK 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034582450 1589 IQYRRSGTEAVLIAHKLNTEEYLRVIGKPAHLIVSLYEHPSINQRIQNSSGTDYPDIHAAAKEIAEVNEINLEKVWDMLL 1668
Cdd:pfam10493  160 RQYQRSKTENLLIAHGLNDEELLKLVGKPAELIVSLYEHSSIEQRYKNPGGRDYPDIHAAVKEIAEINELDLEKIQDMLL 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034582450 1669 EKWLCPSTKP--GEKPSELF-ELQEDEALRRVQYLLLSRPIDYSSRMLFVFATSTTTTLGMHQLTFAHRTRALQCLFYLA 1745
Cdd:pfam10493  240 EKWLCPTMEPtdGTKLEETFlDIQEDEDLRRVVYLLQSWPIDYSVRMLFAIATSETSPLGVNQLTFAHRLRALQCLLKLA 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034582450 1746 DKETIESLFKKPIEEVKSYLRCITFLASFETLNIPITYELFCSSPKEGMIKGLWKNHSHESMAVRLVTELCLEYKIYDLQ 1825
Cdd:pfam10493  320 DGETIESLFKKPIEQVKYYLKCVIFLASFEYLNIPYTYESFHSSPKEGMIKGLWKNHSHEPMAVRLVAELCLEYQVYDPQ 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034582450 1826 LWNGLLQKLLGFNMIPYLRKVLKAISSIHSLWQVPYFSKAWQRVIQIPLLSASCPLSPDQLSDCSESLIAVLECPVSGDL 1905
Cdd:pfam10493  400 LWNGLLQKLLGFNMISYLRKVLDAISSVHSLWQIPGFSRAWQSVILAPLLSASCPLSPDQLEDLYESLVLLLKCPVSDDL 479
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034582450 1906 DLIGVARQYIQLELPAFALACLMLMPHSEKRHQQIKNFLGSCDPQVILKQLEEHMNTGQLAGFSHQIRSLIL 1977
Cdd:pfam10493  480 DLIGIAKQYVQLDLPAFALACLLLIPQSEKRRQQIKKFLSSCNPENLLQQIDELMNTGELAGFASQIRKLVL 551
Rod_C super family cl20400
Rough deal protein C-terminal region; Rod, the Rough deal protein, displays a dynamic ...
334-594 3.10e-50

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: 188.35  E-value: 3.10e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034582450  334 TQEMLNYAKTRLLKKedktALIYSDGLKEVLRAHAKLTTFYGAFGPEKFSGSSWIEFLNNEDdlKDIFLQLKEGNLVCAQ 413
Cdd:pfam10493    1 GIVLPPIAQTRLPFH----LIFTEQPFWKILSAELSEESFPTLLLISKLMKVSLDTLYMSAA--NDVFEKSLKPNSLKEY 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034582450  414 YLWLRHRANFESRFDVKMLESLLNSMSASVSLQKLCPWFKNDVIPFVRRT--VPEGQIILAKWLEQAARNLELTDKAnwp 491
Cdd:pfam10493   75 KSKNSSEANKENNKFLQTILSYLLSIKNPEWAFAIAYKIAQELPEGPDKVeaLYFCLKLAEKWLKNLAPDDEAREKA--- 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034582450  492 ENGLQLAEIFFTAEKTDELGLASswhwiSLKDYQNTEEVCQLRTLVNNLRELITLHRKYNCKLAlSDFEKENTTTIVFRM 571
Cdd:pfam10493  152 EALLKKLKRQYQRSKTENLLIAH-----GLNDEELLKLVGKPAELIVSLYEHSSIEQRYKNPGG-RDYPDIHAAVKEIAE 225
                          250       260
                   ....*....|....*....|...
gi 1034582450  572 FDKVLAPELIPSILEKFIRVYMR 594
Cdd:pfam10493  226 INELDLEKIQDMLLEKWLCPTME 248
 
Name Accession Description Interval E-value
Rod_C pfam10493
Rough deal protein C-terminal region; Rod, the Rough deal protein, displays a dynamic ...
1429-1977 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: 936.02  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034582450 1429 ITLPSAAQTRLPFHLIFfgTAQNFWKILSTELSEESFPTLLLISKLMKFSLDTLYVSTAKHVFEKKLKPKLLKLTQAKSS 1508
Cdd:pfam10493    2 IVLPPIAQTRLPFHLIF--TEQPFWKILSAELSEESFPTLLLISKLMKVSLDTLYMSAANDVFEKSLKPNSLKEYKSKNS 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034582450 1509 TLINKEITKITQTIESCLLSIVNPEWAVAIAISLAQDIPEGSFKISALKFCLYLAERWLQNIPSQDEKREKAEALLKKLH 1588
Cdd:pfam10493   80 SEANKENNKFLQTILSYLLSIKNPEWAFAIAYKIAQELPEGPDKVEALYFCLKLAEKWLKNLAPDDEAREKAEALLKKLK 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034582450 1589 IQYRRSGTEAVLIAHKLNTEEYLRVIGKPAHLIVSLYEHPSINQRIQNSSGTDYPDIHAAAKEIAEVNEINLEKVWDMLL 1668
Cdd:pfam10493  160 RQYQRSKTENLLIAHGLNDEELLKLVGKPAELIVSLYEHSSIEQRYKNPGGRDYPDIHAAVKEIAEINELDLEKIQDMLL 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034582450 1669 EKWLCPSTKP--GEKPSELF-ELQEDEALRRVQYLLLSRPIDYSSRMLFVFATSTTTTLGMHQLTFAHRTRALQCLFYLA 1745
Cdd:pfam10493  240 EKWLCPTMEPtdGTKLEETFlDIQEDEDLRRVVYLLQSWPIDYSVRMLFAIATSETSPLGVNQLTFAHRLRALQCLLKLA 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034582450 1746 DKETIESLFKKPIEEVKSYLRCITFLASFETLNIPITYELFCSSPKEGMIKGLWKNHSHESMAVRLVTELCLEYKIYDLQ 1825
Cdd:pfam10493  320 DGETIESLFKKPIEQVKYYLKCVIFLASFEYLNIPYTYESFHSSPKEGMIKGLWKNHSHEPMAVRLVAELCLEYQVYDPQ 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034582450 1826 LWNGLLQKLLGFNMIPYLRKVLKAISSIHSLWQVPYFSKAWQRVIQIPLLSASCPLSPDQLSDCSESLIAVLECPVSGDL 1905
Cdd:pfam10493  400 LWNGLLQKLLGFNMISYLRKVLDAISSVHSLWQIPGFSRAWQSVILAPLLSASCPLSPDQLEDLYESLVLLLKCPVSDDL 479
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034582450 1906 DLIGVARQYIQLELPAFALACLMLMPHSEKRHQQIKNFLGSCDPQVILKQLEEHMNTGQLAGFSHQIRSLIL 1977
Cdd:pfam10493  480 DLIGIAKQYVQLDLPAFALACLLLIPQSEKRRQQIKKFLSSCNPENLLQQIDELMNTGELAGFASQIRKLVL 551
Rod_C pfam10493
Rough deal protein C-terminal region; Rod, the Rough deal protein, displays a dynamic ...
334-594 3.10e-50

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: 188.35  E-value: 3.10e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034582450  334 TQEMLNYAKTRLLKKedktALIYSDGLKEVLRAHAKLTTFYGAFGPEKFSGSSWIEFLNNEDdlKDIFLQLKEGNLVCAQ 413
Cdd:pfam10493    1 GIVLPPIAQTRLPFH----LIFTEQPFWKILSAELSEESFPTLLLISKLMKVSLDTLYMSAA--NDVFEKSLKPNSLKEY 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034582450  414 YLWLRHRANFESRFDVKMLESLLNSMSASVSLQKLCPWFKNDVIPFVRRT--VPEGQIILAKWLEQAARNLELTDKAnwp 491
Cdd:pfam10493   75 KSKNSSEANKENNKFLQTILSYLLSIKNPEWAFAIAYKIAQELPEGPDKVeaLYFCLKLAEKWLKNLAPDDEAREKA--- 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034582450  492 ENGLQLAEIFFTAEKTDELGLASswhwiSLKDYQNTEEVCQLRTLVNNLRELITLHRKYNCKLAlSDFEKENTTTIVFRM 571
Cdd:pfam10493  152 EALLKKLKRQYQRSKTENLLIAH-----GLNDEELLKLVGKPAELIVSLYEHSSIEQRYKNPGG-RDYPDIHAAVKEIAE 225
                          250       260
                   ....*....|....*....|...
gi 1034582450  572 FDKVLAPELIPSILEKFIRVYMR 594
Cdd:pfam10493  226 INELDLEKIQDMLLEKWLCPTME 248
 
Name Accession Description Interval E-value
Rod_C pfam10493
Rough deal protein C-terminal region; Rod, the Rough deal protein, displays a dynamic ...
1429-1977 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: 936.02  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034582450 1429 ITLPSAAQTRLPFHLIFfgTAQNFWKILSTELSEESFPTLLLISKLMKFSLDTLYVSTAKHVFEKKLKPKLLKLTQAKSS 1508
Cdd:pfam10493    2 IVLPPIAQTRLPFHLIF--TEQPFWKILSAELSEESFPTLLLISKLMKVSLDTLYMSAANDVFEKSLKPNSLKEYKSKNS 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034582450 1509 TLINKEITKITQTIESCLLSIVNPEWAVAIAISLAQDIPEGSFKISALKFCLYLAERWLQNIPSQDEKREKAEALLKKLH 1588
Cdd:pfam10493   80 SEANKENNKFLQTILSYLLSIKNPEWAFAIAYKIAQELPEGPDKVEALYFCLKLAEKWLKNLAPDDEAREKAEALLKKLK 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034582450 1589 IQYRRSGTEAVLIAHKLNTEEYLRVIGKPAHLIVSLYEHPSINQRIQNSSGTDYPDIHAAAKEIAEVNEINLEKVWDMLL 1668
Cdd:pfam10493  160 RQYQRSKTENLLIAHGLNDEELLKLVGKPAELIVSLYEHSSIEQRYKNPGGRDYPDIHAAVKEIAEINELDLEKIQDMLL 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034582450 1669 EKWLCPSTKP--GEKPSELF-ELQEDEALRRVQYLLLSRPIDYSSRMLFVFATSTTTTLGMHQLTFAHRTRALQCLFYLA 1745
Cdd:pfam10493  240 EKWLCPTMEPtdGTKLEETFlDIQEDEDLRRVVYLLQSWPIDYSVRMLFAIATSETSPLGVNQLTFAHRLRALQCLLKLA 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034582450 1746 DKETIESLFKKPIEEVKSYLRCITFLASFETLNIPITYELFCSSPKEGMIKGLWKNHSHESMAVRLVTELCLEYKIYDLQ 1825
Cdd:pfam10493  320 DGETIESLFKKPIEQVKYYLKCVIFLASFEYLNIPYTYESFHSSPKEGMIKGLWKNHSHEPMAVRLVAELCLEYQVYDPQ 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034582450 1826 LWNGLLQKLLGFNMIPYLRKVLKAISSIHSLWQVPYFSKAWQRVIQIPLLSASCPLSPDQLSDCSESLIAVLECPVSGDL 1905
Cdd:pfam10493  400 LWNGLLQKLLGFNMISYLRKVLDAISSVHSLWQIPGFSRAWQSVILAPLLSASCPLSPDQLEDLYESLVLLLKCPVSDDL 479
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034582450 1906 DLIGVARQYIQLELPAFALACLMLMPHSEKRHQQIKNFLGSCDPQVILKQLEEHMNTGQLAGFSHQIRSLIL 1977
Cdd:pfam10493  480 DLIGIAKQYVQLDLPAFALACLLLIPQSEKRRQQIKKFLSSCNPENLLQQIDELMNTGELAGFASQIRKLVL 551
Rod_C pfam10493
Rough deal protein C-terminal region; Rod, the Rough deal protein, displays a dynamic ...
334-594 3.10e-50

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: 188.35  E-value: 3.10e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034582450  334 TQEMLNYAKTRLLKKedktALIYSDGLKEVLRAHAKLTTFYGAFGPEKFSGSSWIEFLNNEDdlKDIFLQLKEGNLVCAQ 413
Cdd:pfam10493    1 GIVLPPIAQTRLPFH----LIFTEQPFWKILSAELSEESFPTLLLISKLMKVSLDTLYMSAA--NDVFEKSLKPNSLKEY 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034582450  414 YLWLRHRANFESRFDVKMLESLLNSMSASVSLQKLCPWFKNDVIPFVRRT--VPEGQIILAKWLEQAARNLELTDKAnwp 491
Cdd:pfam10493   75 KSKNSSEANKENNKFLQTILSYLLSIKNPEWAFAIAYKIAQELPEGPDKVeaLYFCLKLAEKWLKNLAPDDEAREKA--- 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034582450  492 ENGLQLAEIFFTAEKTDELGLASswhwiSLKDYQNTEEVCQLRTLVNNLRELITLHRKYNCKLAlSDFEKENTTTIVFRM 571
Cdd:pfam10493  152 EALLKKLKRQYQRSKTENLLIAH-----GLNDEELLKLVGKPAELIVSLYEHSSIEQRYKNPGG-RDYPDIHAAVKEIAE 225
                          250       260
                   ....*....|....*....|...
gi 1034582450  572 FDKVLAPELIPSILEKFIRVYMR 594
Cdd:pfam10493  226 INELDLEKIQDMLLEKWLCPTME 248
 
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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