ID V5IR03_NEUCR Unreviewed; 1755 AA.
AC V5IR03;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Kinesin {ECO:0000313|EMBL:ESA43571.1};
GN ORFNames=NCU06832 {ECO:0000313|EMBL:ESA43571.1};
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110 {ECO:0000313|EMBL:ESA43571.1, ECO:0000313|Proteomes:UP000001805};
RN [1] {ECO:0000313|EMBL:ESA43571.1, ECO:0000313|Proteomes:UP000001805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987
RC {ECO:0000313|Proteomes:UP000001805};
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.,
RA FitzHugh W., Ma L.J., Smirnov S., Purcell S., Rehman B., Elkins T.,
RA Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D.,
RA Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P., Glass L., Orbach M.J., Berglund J.A., Voelker R., Yarden O.,
RA Plamann M., Seiler S., Dunlap J., Radford A., Aramayo R., Natvig D.O.,
RA Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S.,
RA Lander E.S., Nusbaum C., Birren B.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
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DR EMBL; CM002237; ESA43571.1; -; Genomic_DNA.
DR RefSeq; XP_011393596.1; XM_011395294.1.
DR STRING; 367110.V5IR03; -.
DR PaxDb; 5141-EFNCRP00000006888; -.
DR EnsemblFungi; ESA43571; ESA43571; NCU06832.
DR GeneID; 3879797; -.
DR KEGG; ncr:NCU06832; -.
DR VEuPathDB; FungiDB:NCU06832; -.
DR HOGENOM; CLU_241013_0_0_1; -.
DR InParanoid; V5IR03; -.
DR OMA; WSLKATY; -.
DR OrthoDB; 1430657at2759; -.
DR Proteomes; UP000001805; Chromosome 6, Linkage Group II.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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:0007018; P:microtubule-based movement; IBA:GO_Central.
DR CDD; cd01372; KISc_KIF4; 1.
DR Gene3D; 1.10.287.1490; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR InterPro; IPR027640; Kinesin-like_fam.
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 PANTHER; PTHR47969; CHROMOSOME-ASSOCIATED KINESIN KIF4A-RELATED; 1.
DR PANTHER; PTHR47969:SF33; KINESIN-LIKE PROTEIN; 1.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Reference proteome {ECO:0000313|Proteomes:UP000001805}.
FT DOMAIN 54..443
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 723..809
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 879..898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1564..1627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 564..710
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 945..986
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1049..1125
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1156..1197
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1685..1737
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 7..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..751
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..788
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1564..1594
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 141..148
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1755 AA; 195255 MW; D7F8331251903136 CRC64;
MDFASPPNSP GGSSLPQRPM SAMVRPTQRS SSRMSITSKT GGGSRASDDD VKTAVRVAVR
VRPPLGPDDP GYDLVPQRFQ RSMVQVQGET GVAIDSPQGR KLFVFDRVFG PEVDQEGVWE
YLSDCVNAFT QGYNVSLLAY GQSGAGKSYT MGTAGPDVQE DLEAMGVIPR AAIALFEKLD
GSSPKSQGAA SKRSSMSQLR APSRVAMLQP SNIDKDWKLT ATYVEIYNET LRDLLIPEHI
PQHERGTVTI REDVKGNIIL TGLQQVEVNS VDDLMNVLAQ GSALRQTDAT AINARSSRSH
AVFSLNLVRK GAKGPTAPTD RRMSMPLEAM SGTEAMVTTD SKMHFVDLAG SERLKNTGAQ
GERAKEGISI NAGLAALGKV ISQLSSRQPG AHVSYRDSKL TRLLQDSLGG NAITYMIACV
TQAEFHLSET LNTVQYAQRA RAIQSKPRIQ QVDEGDKQAI IERLKAEVAF LREQIRSSER
GGGDRRSMLL APGERSERQN EREAELQNQL LDARENYTTL SQRHAKLISE MAKARENEFA
ENQHLEESLG ESATERLNRS NSFAQAVEQV VLEYEKTIQS LEQSLASTRA TLANTEATLL
EKETKCAYTE TINTQLQARL QKLMDREAST ENYLHDLEAK LDSHTSGEEK NATIITELRK
EIARVRENEA NAEDYISTLE ERLAEADQDA ELMQREIDRL EQVIERQRSL GKLDSLLNEL
DHIQQDPPTI PENEHELTNG GRHRKMASRD YANHSRSQSH VSHRSQFDEP IRESSEEDIP
EEDEDNLDAT PTDKANTPKA SHAQLAGKNG SKLVPVDQFE TVTKELVDLR TEHETTLHDY
SALQAKHEEA LRALAELQDA VDEARHPSRV RDSILSVSAP GTRPMSLMSG ETKTGHRSLS
SELSSALGSH TVVTDVSGAE TAKHHDSEID EADADAQIQK LKFIAAAKEA AERELATRYA
QLEEKHQETL DMVEELKTEI AKAQALSVES SISRTSTPVI RRKSSQNVMI IDRAHRSFAT
LSNIAAENLH DPDVMANFEL NLNAAMHELH ARSVRIQELE ADVTNAKKEM ETKMTIISGL
TRERSSLKAA SPMDMAMVSS LREQLERSEK HVQELRESNA IRQRELEAQI SELQHALHQA
GVDPASVGPR VFDGDSDAQA KRIVELEAEL RGWEAKHQAA LENLQDSENR MKSSMAELGS
QISFLTTQLT ETETQSSMLS SRLAQTEGQV TSLNDQLAQN GHKEPEGDEA AKEKKHKELV
EVLRREIDDY KEIVNRTQTK VTQTEEQAAA TKVLLDAATR ERDDAAAEAE HNKQLVNRLE
ESITEHEHTI KAHQESLHAL ELNHALELEE ARTASRREVE AEMKALKAKH AEQVRRLEEG
LTDAREDLLR VATQVALALG LEVSIEKLSE RIEDLLESRD QVDLEQKKRG ELEQHVVELT
SINDQVMNEL ESVKAALADM LATENDKVKT VYPVKESVAL VKKKMVDLET KNKKNSRLVE
ELEDQLQSNY DQVQITSNRL SMLQSEKTQQ LEEANAAIIR LEEELKMARE EYAALQTKYN
VLSEQAASVP QRSDSKSAPN PSSPIRKSNS VQSLPSPPPA IPLPPLPSDR ASGAVSPTSG
APRPPSKDIL AAALSNQQFQ AIQEDQEARI RIIEKNLLAE KQLTATLEEA LTDLETQQLK
IKADADAWKR RAGELEAELK ELKDKPQVDN RWSLQQVEEE RKKRVDAERA RQHLEERMQS
LASGKKKKKG SLNCF
//
