ID   KLPA_EMENI              Reviewed;         770 AA.
AC   P28739; C8V100; Q5AZE0;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2011, sequence version 3.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Kinesin-like protein klpA;
GN   Name=klpA; ORFNames=AN6340;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=GB20;
RX   PubMed=8416986; DOI=10.1083/jcb.120.1.153;
RA   O'Connell M.J., Meluh P.B., Rose M.D., Morris N.R.;
RT   "Suppression of the bimC4 mitotic spindle defect by deletion of klpA, a
RT   gene encoding a KAR3-related kinesin-like protein in Aspergillus
RT   nidulans.";
RL   J. Cell Biol. 120:153-162(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. NCD subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00283}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAA58724.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; X64603; CAA45887.1; -; mRNA.
DR   EMBL; AACD01000107; EAA58724.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BN001301; CBF69667.1; -; Genomic_DNA.
DR   PIR; A44337; A44337.
DR   RefSeq; XP_663944.1; XM_658852.1.
DR   AlphaFoldDB; P28739; -.
DR   SMR; P28739; -.
DR   STRING; 162425.CADANIAP00006645; -.
DR   PRIDE; P28739; -.
DR   EnsemblFungi; CBF69667; CBF69667; ANIA_06340.
DR   EnsemblFungi; EAA58724; EAA58724; AN6340.2.
DR   GeneID; 2871239; -.
DR   KEGG; ani:AN6340.2; -.
DR   VEuPathDB; FungiDB:AN6340; -.
DR   eggNOG; KOG0239; Eukaryota.
DR   HOGENOM; CLU_001485_12_1_1; -.
DR   InParanoid; P28739; -.
DR   OMA; RHDMQKC; -.
DR   OrthoDB; 364605at2759; -.
DR   Proteomes; UP000000560; Chromosome I.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0000235; C:astral microtubule; IEA:EnsemblFungi.
DR   GO; GO:0055028; C:cortical microtubule; IEA:EnsemblFungi.
DR   GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR   GO; GO:0000776; C:kinetochore; IEA:EnsemblFungi.
DR   GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR   GO; GO:0036449; C:microtubule minus-end; IEA:EnsemblFungi.
DR   GO; GO:0005815; C:microtubule organizing center; IBA:GO_Central.
DR   GO; GO:0035371; C:microtubule plus-end; IEA:EnsemblFungi.
DR   GO; GO:0005872; C:minus-end kinesin complex; IEA:EnsemblFungi.
DR   GO; GO:0072686; C:mitotic spindle; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR   GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR   GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR   GO; GO:0008569; F:minus-end-directed microtubule motor activity; IDA:AspGD.
DR   GO; GO:0008574; F:plus-end-directed microtubule motor activity; IEA:EnsemblFungi.
DR   GO; GO:0031122; P:cytoplasmic microtubule organization; IEA:EnsemblFungi.
DR   GO; GO:0030951; P:establishment or maintenance of microtubule cytoskeleton polarity; IEA:EnsemblFungi.
DR   GO; GO:0000742; P:karyogamy involved in conjugation with cellular fusion; IEA:EnsemblFungi.
DR   GO; GO:1990571; P:meiotic centromere clustering; IEA:EnsemblFungi.
DR   GO; GO:0140642; P:meiotic spindle formation (spindle phase two); IEA:EnsemblFungi.
DR   GO; GO:1990810; P:microtubule anchoring at mitotic spindle pole body; IEA:EnsemblFungi.
DR   GO; GO:0001578; P:microtubule bundle formation; IEA:EnsemblFungi.
DR   GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR   GO; GO:0031534; P:minus-end directed microtubule sliding; IEA:EnsemblFungi.
DR   GO; GO:1990942; P:mitotic metaphase chromosome recapture; IEA:EnsemblFungi.
DR   GO; GO:0090307; P:mitotic spindle assembly; IMP:AspGD.
DR   GO; GO:0140641; P:mitotic spindle formation (spindle phase two); IEA:EnsemblFungi.
DR   GO; GO:0051256; P:mitotic spindle midzone assembly; IEA:EnsemblFungi.
DR   GO; GO:0090561; P:nuclear migration during mitotic telophase; IEA:EnsemblFungi.
DR   GO; GO:0031535; P:plus-end directed microtubule sliding; IEA:EnsemblFungi.
DR   Gene3D; 3.40.850.10; -; 1.
DR   InterPro; IPR019821; Kinesin_motor_CS.
DR   InterPro; IPR001752; Kinesin_motor_dom.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00225; Kinesin; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00129; KISc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton; Microtubule;
KW   Motor protein; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..770
FT                   /note="Kinesin-like protein klpA"
FT                   /id="PRO_0000125384"
FT   DOMAIN          421..756
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   REGION          1..152
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          175..425
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        44..59
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        70..120
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         514..521
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   770 AA;  85801 MW;  EFD0F0FF39B5C7EB CRC64;
     MENVQSRMQG SRIPGLKEMN PSGTNARSRL PQPGAIANKP TAVPQLARTR STTESTRIGA
     GPPSAARSVN GATKAHTRAN SYANSSTLTR SASAASRPRG PLSSSTSGRP KTSMSTSRRP
     NGHALPRPAT SLDTHQEERS YGGLGKRGEW DQDEREQNLE SLFETFVSRI SQQGQESSGL
     KDALEVYKSR VGELEEAKSE QTEQNIRLKV ELDVSKSRLA EAEDALKNAQ RDHEIAIDEL
     MSRQRAECES VRYESQKSLD ALKAQHESEL KELRRQFERE LEDEKCARVR ELNQLHSKTA
     LDAQLSQIEL DKTIKELAAT REDLQSLRTE LDRERKNTNN LRQNLDTAAS NSVTLESTIS
     ALKARIEFLE SGREEQSEAF ERLNQQMMDA MAETNAAKEK LRREETLRRK LHNQVQELKG
     NIRVFCRVRP TLENEGASDA AQFTYPDEGE DSKEINIIGP EEKSSFGTVT RKNHNFSFDH
     VFGPSAQNSD VFDEISQLVQ SALDGYNVCI FCYGQTGSGK THTMSSLDGM IPRAVHQIYE
     TATSLEEKGW RYTMEGNFVE VYNENLNDLL GKAEELDKKK LEIRHDMQRG KTTITDATTV
     QLESPEMVES LLKRAAANRS VAATKANERS SRSHSIFILK LIGENYITGE RSEGTLNLVD
     LAGSERLSHS GATGDRLKET QNINRSLSCL GDVIAALGQG KKDGHIPYRN SKLTYLLQFS
     LGGNSKTLMF VMVSPLQAHL SETLTSLKFA TKVHNTHIGT AKKQTRVRDV