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Protein

Kinesin-like protein Nod

Gene

nod

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Required for the distributive chromosome segregation of non-exchange chromosomes during meiosis. May be a microtubule motor required to hold distributively "paired" chromosomes at the metaphase plate until anaphase.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi87 – 948ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATPase activity Source: GO_Central
  • ATP binding Source: UniProtKB-KW
  • microtubule motor activity Source: UniProtKB
  • microtubule plus-end binding Source: FlyBase

GO - Biological processi

  • distributive segregation Source: FlyBase
  • establishment of meiotic spindle orientation Source: FlyBase
  • female meiotic division Source: FlyBase
  • meiotic chromosome segregation Source: UniProtKB
  • microtubule-based movement Source: GO_Central
  • mitotic spindle organization Source: FlyBase
  • positive regulation of microtubule polymerization Source: FlyBase
  • spindle assembly involved in female meiosis I Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Motor protein

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Kinesin-like protein Nod
Gene namesi
Name:nod
Synonyms:NODA
ORF Names:CG1763
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0002948. nod.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-KW
  • kinesin complex Source: UniProtKB
  • microtubule Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 666666Kinesin-like protein NodPRO_0000125426Add
BLAST

Proteomic databases

PaxDbiP18105.
PRIDEiP18105.

Expressioni

Tissue specificityi

In adult female, found in meiotically active ovaries.

Developmental stagei

Embryonic, larval, and pupal stages. Only expressed in female adults.

Gene expression databases

BgeeiP18105.
GenevisibleiP18105. DM.

Interactioni

GO - Molecular functioni

  • microtubule plus-end binding Source: FlyBase

Protein-protein interaction databases

BioGridi58516. 6 interactions.
DIPiDIP-22708N.
IntActiP18105. 1 interaction.
MINTiMINT-825971.
STRINGi7227.FBpp0073363.

Structurei

Secondary structure

1
666
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 159Combined sources
Beta strandi29 – 313Combined sources
Beta strandi34 – 363Combined sources
Beta strandi38 – 436Combined sources
Beta strandi46 – 494Combined sources
Beta strandi51 – 544Combined sources
Helixi60 – 678Combined sources
Helixi69 – 779Combined sources
Beta strandi81 – 888Combined sources
Helixi93 – 975Combined sources
Helixi102 – 1043Combined sources
Helixi107 – 1093Combined sources
Helixi112 – 12615Combined sources
Beta strandi127 – 1304Combined sources
Beta strandi136 – 14712Combined sources
Beta strandi149 – 1513Combined sources
Turni165 – 1673Combined sources
Beta strandi172 – 1765Combined sources
Helixi177 – 18913Combined sources
Beta strandi205 – 21410Combined sources
Beta strandi219 – 2268Combined sources
Helixi252 – 26413Combined sources
Helixi272 – 2743Combined sources
Helixi276 – 2805Combined sources
Turni281 – 2844Combined sources
Beta strandi290 – 2978Combined sources
Helixi301 – 3033Combined sources
Helixi304 – 31815Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DC4X-ray1.90A1-318[»]
3DCBX-ray2.50A1-318[»]
3DCOelectron microscopy1.90N1-318[»]
3PXNX-ray2.60A1-322[»]
ProteinModelPortaliP18105.
SMRiP18105. Positions 5-318.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP18105.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini8 – 320313Kinesin motorPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili639 – 66628Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family.PROSITE-ProRule annotation
Contains 1 kinesin motor domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG0244. Eukaryota.
COG5059. LUCA.
HOGENOMiHOG000244977.
InParanoidiP18105.
OMAiQRTRSEM.
OrthoDBiEOG7NW69G.
PhylomeDBiP18105.

Family and domain databases

Gene3Di3.40.850.10. 1 hit.
InterProiIPR027640. Kinesin-like_fam.
IPR019821. Kinesin_motor_CS.
IPR001752. Kinesin_motor_dom.
IPR027417. P-loop_NTPase.
IPR010994. RuvA_2-like.
[Graphical view]
PANTHERiPTHR24115. PTHR24115. 2 hits.
PfamiPF00225. Kinesin. 1 hit.
[Graphical view]
PRINTSiPR00380. KINESINHEAVY.
SMARTiSM00129. KISc. 1 hit.
[Graphical view]
SUPFAMiSSF47781. SSF47781. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS00411. KINESIN_MOTOR_1. 1 hit.
PS50067. KINESIN_MOTOR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P18105-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEGAKLSAVR IAVREAPYRQ FLGRREPSVV QFPPWSDGKS LIVDQNEFHF
60 70 80 90 100
DHAFPATISQ DEMYQALILP LVDKLLEGFQ CTALAYGQTG TGKSYSMGMT
110 120 130 140 150
PPGEILPEHL GILPRALGDI FERVTARQEN NKDAIQVYAS FIEIYNEKPF
160 170 180 190 200
DLLGSTPHMP MVAARCQRCT CLPLHSQADL HHILELGTRN RRVRPTNMNS
210 220 230 240 250
NSSRSHAIVT IHVKSKTHHS RMNIVDLAGS EGVRRTGHEG VARQEGVNIN
260 270 280 290 300
LGLLSINKVV MSMAAGHTVI PYRDSVLTTV LQASLTAQSY LTFLACISPH
310 320 330 340 350
QCDLSETLST LRFGTSAKKL RLNPMQVARQ KQSLAARTTH VFRQALCTST
360 370 380 390 400
AIKSNAANHN SIVVPKSKYS TTKPLSAVLH RTRSELGMTP KAKKRARELL
410 420 430 440 450
ELEETTLELS SIHIQDSSLS LLGFHSDSDK DRHLMPPPTG QEPRQASSQN
460 470 480 490 500
STLMGIVEET EPKESSKVQQ SMVAPTVPTT VRCQLFNTTI SPISLRASSS
510 520 530 540 550
QRELSGIQPM EETVVASPQQ PCLRRSVRLA SSMRSQNYGA IPKVMNLRRS
560 570 580 590 600
TRLAGIREHA TSVVVKNETD AIPHLRSTVQ KKRTRNVKPA PKAWMANNTK
610 620 630 640 650
CFLDLLNNGN VKQLQEIPGI GPKSAFSLAL HRSRLGCFEN LFQVKSLPIW
660
SGNKWERFCQ INCLDT
Length:666
Mass (Da):73,908
Last modified:November 1, 1990 - v1
Checksum:iE3DEF72C08973FC2
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti94 – 941S → N in allele NOD(DTW).

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M36195 Genomic DNA. Translation: AAA28653.1.
M94188 Genomic DNA. Translation: AAC14452.1.
AE014298 Genomic DNA. Translation: AAF48064.2.
AY050238 mRNA. Translation: AAK84937.1.
PIRiA36026.
RefSeqiNP_001285129.1. NM_001298200.1.
NP_511125.2. NM_078570.3.
UniGeneiDm.139.

Genome annotation databases

EnsemblMetazoaiFBtr0073516; FBpp0073363; FBgn0002948.
FBtr0340297; FBpp0309258; FBgn0002948.
GeneIDi32107.
KEGGidme:Dmel_CG1763.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M36195 Genomic DNA. Translation: AAA28653.1.
M94188 Genomic DNA. Translation: AAC14452.1.
AE014298 Genomic DNA. Translation: AAF48064.2.
AY050238 mRNA. Translation: AAK84937.1.
PIRiA36026.
RefSeqiNP_001285129.1. NM_001298200.1.
NP_511125.2. NM_078570.3.
UniGeneiDm.139.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DC4X-ray1.90A1-318[»]
3DCBX-ray2.50A1-318[»]
3DCOelectron microscopy1.90N1-318[»]
3PXNX-ray2.60A1-322[»]
ProteinModelPortaliP18105.
SMRiP18105. Positions 5-318.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi58516. 6 interactions.
DIPiDIP-22708N.
IntActiP18105. 1 interaction.
MINTiMINT-825971.
STRINGi7227.FBpp0073363.

Proteomic databases

PaxDbiP18105.
PRIDEiP18105.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0073516; FBpp0073363; FBgn0002948.
FBtr0340297; FBpp0309258; FBgn0002948.
GeneIDi32107.
KEGGidme:Dmel_CG1763.

Organism-specific databases

CTDi32107.
FlyBaseiFBgn0002948. nod.

Phylogenomic databases

eggNOGiKOG0244. Eukaryota.
COG5059. LUCA.
HOGENOMiHOG000244977.
InParanoidiP18105.
OMAiQRTRSEM.
OrthoDBiEOG7NW69G.
PhylomeDBiP18105.

Miscellaneous databases

EvolutionaryTraceiP18105.
GenomeRNAii32107.
PROiP18105.

Gene expression databases

BgeeiP18105.
GenevisibleiP18105. DM.

Family and domain databases

Gene3Di3.40.850.10. 1 hit.
InterProiIPR027640. Kinesin-like_fam.
IPR019821. Kinesin_motor_CS.
IPR001752. Kinesin_motor_dom.
IPR027417. P-loop_NTPase.
IPR010994. RuvA_2-like.
[Graphical view]
PANTHERiPTHR24115. PTHR24115. 2 hits.
PfamiPF00225. Kinesin. 1 hit.
[Graphical view]
PRINTSiPR00380. KINESINHEAVY.
SMARTiSM00129. KISc. 1 hit.
[Graphical view]
SUPFAMiSSF47781. SSF47781. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS00411. KINESIN_MOTOR_1. 1 hit.
PS50067. KINESIN_MOTOR_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A kinesin-like protein required for distributive chromosome segregation in Drosophila."
    Zhang P., Knowles B.A., Goldstein L.S.B., Hawley R.S.
    Cell 62:1053-1062(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Oregon-R.
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  5. "The lethal(1)TW-6cs mutation of Drosophila melanogaster is a dominant antimorphic allele of nod and is associated with a single base change in the putative ATP-binding domain."
    Rasooly R.S., New C.M., Zhang P., Hawley R.S., Baker B.S.
    Genetics 129:409-422(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ALLELE NOD(DTW).

Entry informationi

Entry nameiNOD_DROME
AccessioniPrimary (citable) accession number: P18105
Secondary accession number(s): Q9VYW9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: July 6, 2016
This is version 150 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Miscellaneous

The nod(DTW) mutation is a cold-sensitive recessive lethal mutation.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.