NUCLEOTIDE SEQUENCE.
DOI=10.1128/EC.3.3.632-645.2004; PubMed=15189985 [NCBI, ExPASy, EBI, Israel, Japan]
Rischitor P.E., Konzack S., Fischer R.;
"The Kip3-like kinesin KipB moves along microtubules and determines spindle position during synchronized mitoses in Aspergillus nidulans hyphae.";
Eukaryot. Cell 3:632-645(2004).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=FGSC 4;
DOI=10.1038/nature04341; PubMed=16372000 [NCBI, ExPASy, EBI, Israel, Japan]
Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae.";
Nature 438:1105-1115(2005).

Comments

SIMILARITY: Belongs to the kinesin-like protein family.
SIMILARITY: Contains 1 kinesin-motor domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AJ620863; CAF06507.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AACD01000078; EAA60856.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

XP_662117.1; -.

3D structure databases

ModBase

Q704T4.

Ontologies

GO:0005875;	Cellular component: microtubule associated complex (inferred from electronic annotation from InterPro).
GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0003777;	Molecular function: microtubule motor activity (inferred from electronic annotation from InterPro).
GO:0007018;	Biological process: microtubule-based movement (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR001752; Kinesin_motor.
IPR019821; Kinesin_motor_CS.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.850.10; kinesin_motor; 1.

Pfam

PF00225; Kinesin; 1.
Pfam graphical view of domain structure.

PRINTS

PR00380; KINESINHEAVY.

SMART

SM00129; KISc; 1.
SMART graphical view of domain structure.

PROSITE

PS00411; KINESIN_MOTOR_DOMAIN1; 1.
PS50067; KINESIN_MOTOR_DOMAIN2; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

GeneID

2872311; -.

KEGG

ani:AN4513.2; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

ATP-binding; Microtubule; Motor protein; Nucleotide-binding.

Features

None

Sequence information

Length: 989 AA

Molecular weight: 108674 Da

CRC64: 7FD480C6D0A815AB [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGASSDSSSI SVTVRVRPFT IREAAQLTKC EDGPLFLGDG SLAGAPAPKL NQKGLRSIIK 

        70         80         90        100        110        120 
VIDDRCLVFD PPEDNPVQKF SRSVVPNGKR VKDQTFAFDR IFDQNATQGE VYEATTRSLL 

       130        140        150        160        170        180 
DSVLDGYNAT VFAYGATGCG KTHTITGTPQ QPGIIFLTMQ ELFERIEERK SEKHTELSLS 

       190        200        210        220        230        240 
FLEIYNETIR DLLVPGGAKS GLSLREDSNK AVSVSGLSSH SPKSVQEVMD MIMKGNACRT 

       250        260        270        280        290        300 
MSPTEANATS SRSHAVLQIN VAQKDRNADI NEPHTMATFS IIDLAGSERA SATKNRGERL 

       310        320        330        340        350        360 
FEGANINKSL LALGSCINAL CDPRKRNHVP YRNSKLTRLL KFSLGGNCKT VMIVCVSPSS 

       370        380        390        400        410        420 
QHFDETQNTL RYANRAKNIQ TKVTRNVFNV NRHVKDFLVK IDEQMALINE LKAQQRESEK 

       430        440        450        460        470        480 
VAFAKFKKQT EKKDAAVREG LARIRNAYDH SLPERQERIN NMIRLKQVSR RIGLLSSWIA 

       490        500        510        520        530        540 
AFDNVCANSE NEVPLSNLQA VRKTAQGILL ELEGSRQHYH QRLAKSTWDR GMTSAVENAV 

       550        560        570        580        590        600 
QQLQEFDTSD KSDVTNLRRE AELLRANTER EALSAVAEQD KAGDAAVVQL LLQAHFEIAS 

       610        620        630        640        650        660 
SIERIMHLSE EEAVEMGKRS LTKMLDSCCT ATSNVVKPDS NLPPMPTFSP SKHSPAKAKK 

       670        680        690        700        710        720 
RLSLAIVPPS KSLNATVALH PTAPTSPTRG SPRRRKMGTG RKSVSFSPKK APAKPPKRSV 

       730        740        750        760        770        780 
RWKDDEEDGT LTEIQKTPQK REATLIHRSV SPQEPGLPRA SPIPRGIPVP TRNFSPSGGS 

       790        800        810        820        830        840 
SPIPTPSDQP LSIPKNNRFK TGFLSKKTGS SPIPAPPTVA LSVSDRSSPL RDIEGSSFLN 

       850        860        870        880        890        900 
RASTERPSRI AVRTPSGNYS PSPAQPETKG EWKASKDDVR RISTAMRRIS IGSFGTSASA 

       910        920        930        940        950        960 
TALRAHRRRS PTSATYGSSP PENTMFTAQA RRMAKGEKEL ENKPAVLGPR SLPIKKNTSQ 

       970        980 
RRTTFGGDIR PRDFSFSGRD IRLSAIGGF

Q704T4 in FASTA format

View entry in raw text format (no links)
Request for annotation of this UniProtKB/TrEMBL entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools