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Conserved domains on  [gi|568254179|gb|ETN63171|]
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rough deal [Anopheles darlingi]

Protein Classification

Rod_C domain-containing protein( domain architecture ID 10564672)

Rod_C domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Rod_C super family cl20400
Rough deal protein C-terminal region; Rod, the Rough deal protein, displays a dynamic ...
986-1531 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.


The actual alignment was detected with superfamily member pfam10493:

Pssm-ID: 463114  Cd Length: 551  Bit Score: 625.16  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568254179   986 GDMLPEIAKYRYPFMLIV-RQPLKQLLKEEIAIDNYQKLLVLVE-MKCALEGFDCNEMNDNFCKSAVVNSINEYKIQNKE 1063
Cdd:pfam10493    1 GIVLPPIAQTRLPFHLIFtEQPFWKILSAELSEESFPTLLLISKlMKVSLDTLYMSAANDVFEKSLKPNSLKEYKSKNSS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568254179  1064 MAlahndwhrQAKNKAFLQSILRIVDSIKDLSSRLFILYYITCNASDGDDQVNAAYACYTFARKHETELASMPEAKEK-- 1141
Cdd:pfam10493   81 EA--------NKENNKFLQTILSYLLSIKNPEWAFAIAYKIAQELPEGPDKVEALYFCLKLAEKWLKNLAPDDEAREKae 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568254179  1142 --LEKIFRKYPLLKTQQLLQQNGVTEEKQFQLVRNPHELIMALYSDSCFQQV----------KVNELVSVIGELYELDIE 1209
Cdd:pfam10493  153 alLKKLKRQYQRSKTENLLIAHGLNDEELLKLVGKPAELIVSLYEHSSIEQRyknpggrdypDIHAAVKEIAEINELDLE 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568254179  1210 GIQMQLLQKWLTIFGGTTSensASMLEETLYDDHnmsdasqedeegVHEYMKRAYYILSSWERSKSVEFLVAQLNTSTDG 1289
Cdd:pfam10493  233 KIQDMLLEKWLCPTMEPTD---GTKLEETFLDIQ------------EDEDLRRVVYLLQSWPIDYSVRMLFAIATSETSP 297
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568254179  1290 VS---SDVGKQLHIYQCFSKLVDEECN--PYQTFFTQQRYVaLKCVHLLKSLGLGNL--SIAKFEETDKMALLKMLWQSH 1362
Cdd:pfam10493  298 LGvnqLTFAHRLRALQCLLKLADGETIesLFKKPIEQVKYY-LKCVIFLASFEYLNIpyTYESFHSSPKEGMIKGLWKNH 376
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568254179  1363 ASNPKGLEVIALICIGYNIYLPQIWNGILKQMARLGMVANLRALIDIVTAKRQLFGLEGYRMAWELLIEQPFRSASREQS 1442
Cdd:pfam10493  377 SHEPMAVRLVAELCLEYQVYDPQLWNGLLQKLLGFNMISYLRKVLDAISSVHSLWQIPGFSRAWQSVILAPLLSASCPLS 456
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568254179  1443 LAEDALLARSLVMVQRCPISFRLNLLEIARECVTVNRVNMA--AVLIGFADSEQKETLKKLIANNAVPNLKDQIQEL--- 1517
Cdd:pfam10493  457 PDQLEDLYESLVLLLKCPVSDDLDLIGIAKQYVQLDLPAFAlaCLLLIPQSEKRRQQIKKFLSSCNPENLLQQIDELmnt 536
                          570
                   ....*....|....*
gi 568254179  1518 -EEFGLVTTITKAVC 1531
Cdd:pfam10493  537 gELAGFASQIRKLVL 551
 
Name Accession Description Interval E-value
Rod_C pfam10493
Rough deal protein C-terminal region; Rod, the Rough deal protein, displays a dynamic ...
986-1531 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: 625.16  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568254179   986 GDMLPEIAKYRYPFMLIV-RQPLKQLLKEEIAIDNYQKLLVLVE-MKCALEGFDCNEMNDNFCKSAVVNSINEYKIQNKE 1063
Cdd:pfam10493    1 GIVLPPIAQTRLPFHLIFtEQPFWKILSAELSEESFPTLLLISKlMKVSLDTLYMSAANDVFEKSLKPNSLKEYKSKNSS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568254179  1064 MAlahndwhrQAKNKAFLQSILRIVDSIKDLSSRLFILYYITCNASDGDDQVNAAYACYTFARKHETELASMPEAKEK-- 1141
Cdd:pfam10493   81 EA--------NKENNKFLQTILSYLLSIKNPEWAFAIAYKIAQELPEGPDKVEALYFCLKLAEKWLKNLAPDDEAREKae 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568254179  1142 --LEKIFRKYPLLKTQQLLQQNGVTEEKQFQLVRNPHELIMALYSDSCFQQV----------KVNELVSVIGELYELDIE 1209
Cdd:pfam10493  153 alLKKLKRQYQRSKTENLLIAHGLNDEELLKLVGKPAELIVSLYEHSSIEQRyknpggrdypDIHAAVKEIAEINELDLE 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568254179  1210 GIQMQLLQKWLTIFGGTTSensASMLEETLYDDHnmsdasqedeegVHEYMKRAYYILSSWERSKSVEFLVAQLNTSTDG 1289
Cdd:pfam10493  233 KIQDMLLEKWLCPTMEPTD---GTKLEETFLDIQ------------EDEDLRRVVYLLQSWPIDYSVRMLFAIATSETSP 297
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568254179  1290 VS---SDVGKQLHIYQCFSKLVDEECN--PYQTFFTQQRYVaLKCVHLLKSLGLGNL--SIAKFEETDKMALLKMLWQSH 1362
Cdd:pfam10493  298 LGvnqLTFAHRLRALQCLLKLADGETIesLFKKPIEQVKYY-LKCVIFLASFEYLNIpyTYESFHSSPKEGMIKGLWKNH 376
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568254179  1363 ASNPKGLEVIALICIGYNIYLPQIWNGILKQMARLGMVANLRALIDIVTAKRQLFGLEGYRMAWELLIEQPFRSASREQS 1442
Cdd:pfam10493  377 SHEPMAVRLVAELCLEYQVYDPQLWNGLLQKLLGFNMISYLRKVLDAISSVHSLWQIPGFSRAWQSVILAPLLSASCPLS 456
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568254179  1443 LAEDALLARSLVMVQRCPISFRLNLLEIARECVTVNRVNMA--AVLIGFADSEQKETLKKLIANNAVPNLKDQIQEL--- 1517
Cdd:pfam10493  457 PDQLEDLYESLVLLLKCPVSDDLDLIGIAKQYVQLDLPAFAlaCLLLIPQSEKRRQQIKKFLSSCNPENLLQQIDELmnt 536
                          570
                   ....*....|....*
gi 568254179  1518 -EEFGLVTTITKAVC 1531
Cdd:pfam10493  537 gELAGFASQIRKLVL 551
 
Name Accession Description Interval E-value
Rod_C pfam10493
Rough deal protein C-terminal region; Rod, the Rough deal protein, displays a dynamic ...
986-1531 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: 625.16  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568254179   986 GDMLPEIAKYRYPFMLIV-RQPLKQLLKEEIAIDNYQKLLVLVE-MKCALEGFDCNEMNDNFCKSAVVNSINEYKIQNKE 1063
Cdd:pfam10493    1 GIVLPPIAQTRLPFHLIFtEQPFWKILSAELSEESFPTLLLISKlMKVSLDTLYMSAANDVFEKSLKPNSLKEYKSKNSS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568254179  1064 MAlahndwhrQAKNKAFLQSILRIVDSIKDLSSRLFILYYITCNASDGDDQVNAAYACYTFARKHETELASMPEAKEK-- 1141
Cdd:pfam10493   81 EA--------NKENNKFLQTILSYLLSIKNPEWAFAIAYKIAQELPEGPDKVEALYFCLKLAEKWLKNLAPDDEAREKae 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568254179  1142 --LEKIFRKYPLLKTQQLLQQNGVTEEKQFQLVRNPHELIMALYSDSCFQQV----------KVNELVSVIGELYELDIE 1209
Cdd:pfam10493  153 alLKKLKRQYQRSKTENLLIAHGLNDEELLKLVGKPAELIVSLYEHSSIEQRyknpggrdypDIHAAVKEIAEINELDLE 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568254179  1210 GIQMQLLQKWLTIFGGTTSensASMLEETLYDDHnmsdasqedeegVHEYMKRAYYILSSWERSKSVEFLVAQLNTSTDG 1289
Cdd:pfam10493  233 KIQDMLLEKWLCPTMEPTD---GTKLEETFLDIQ------------EDEDLRRVVYLLQSWPIDYSVRMLFAIATSETSP 297
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568254179  1290 VS---SDVGKQLHIYQCFSKLVDEECN--PYQTFFTQQRYVaLKCVHLLKSLGLGNL--SIAKFEETDKMALLKMLWQSH 1362
Cdd:pfam10493  298 LGvnqLTFAHRLRALQCLLKLADGETIesLFKKPIEQVKYY-LKCVIFLASFEYLNIpyTYESFHSSPKEGMIKGLWKNH 376
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568254179  1363 ASNPKGLEVIALICIGYNIYLPQIWNGILKQMARLGMVANLRALIDIVTAKRQLFGLEGYRMAWELLIEQPFRSASREQS 1442
Cdd:pfam10493  377 SHEPMAVRLVAELCLEYQVYDPQLWNGLLQKLLGFNMISYLRKVLDAISSVHSLWQIPGFSRAWQSVILAPLLSASCPLS 456
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568254179  1443 LAEDALLARSLVMVQRCPISFRLNLLEIARECVTVNRVNMA--AVLIGFADSEQKETLKKLIANNAVPNLKDQIQEL--- 1517
Cdd:pfam10493  457 PDQLEDLYESLVLLLKCPVSDDLDLIGIAKQYVQLDLPAFAlaCLLLIPQSEKRRQQIKKFLSSCNPENLLQQIDELmnt 536
                          570
                   ....*....|....*
gi 568254179  1518 -EEFGLVTTITKAVC 1531
Cdd:pfam10493  537 gELAGFASQIRKLVL 551
 
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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