ID V5IMM6_NEUCR Unreviewed; 1877 AA.
AC V5IMM6;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Kinesin {ECO:0000313|EMBL:ESA42610.1};
GN Name=nkin-2 {ECO:0000313|EMBL:ESA42610.1};
GN ORFNames=NCU06733 {ECO:0000313|EMBL:ESA42610.1};
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:ESA42610.1, ECO:0000313|Proteomes:UP000001805};
RN [1] {ECO:0000313|EMBL:ESA42610.1, 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 -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM002240; ESA42610.1; -; Genomic_DNA.
DR RefSeq; XP_011394712.1; XM_011396410.1.
DR STRING; 367110.V5IMM6; -.
DR PaxDb; 5141-EFNCRP00000006600; -.
DR EnsemblFungi; ESA42610; ESA42610; NCU06733.
DR GeneID; 3876808; -.
DR VEuPathDB; FungiDB:NCU06733; -.
DR InParanoid; V5IMM6; -.
DR OrthoDB; 126886at2759; -.
DR Proteomes; UP000001805; Chromosome 2, Linkage Group V.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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:0030705; P:cytoskeleton-dependent intracellular transport; IBA:GO_Central.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR CDD; cd22705; FHA_KIF1; 1.
DR CDD; cd01365; KISc_KIF1A_KIF1B; 1.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 6.10.250.2520; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR022164; Kinesin-like.
DR InterPro; IPR022140; Kinesin-like_KIF1-typ.
DR InterPro; IPR032405; Kinesin_assoc.
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 InterPro; IPR001849; PH_domain.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR PANTHER; PTHR47117:SF3; KINESIN FAMILY MEMBER 14-LIKE; 1.
DR PANTHER; PTHR47117; STAR-RELATED LIPID TRANSFER PROTEIN 9; 1.
DR Pfam; PF12473; DUF3694; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF12423; KIF1B; 1.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF16183; Kinesin_assoc; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00240; FHA; 1.
DR SMART; SM00129; KISc; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00283};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00283}; Reference proteome {ECO:0000313|Proteomes:UP000001805}.
FT DOMAIN 13..364
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT DOMAIN 1572..1833
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 630..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1420..1509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1663..1704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1724..1791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1837..1877
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 770..821
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 630..667
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1490..1509
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1685..1704
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1727..1791
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1862..1877
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 110..117
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1877 AA; 206665 MW; CD2037E492D9A6EA CRC64;
MAPGMAPMGG GGNIKVVVRC RPFNAREHDR GAQCIVEMRD NQTVLTTPPD AVVKGGKDQG
QKIFAFDRSY WSFDKNAPNY AGQDQLHEDL GKPLLDNAFQ GYNNCIFAYG QTGSGKSYSM
MGYGKDAGII PMICQDMFKR INDMQQDKNL RCTVEVSYLE IYNERVRDLL NPANKGNLKV
REHPSTGPYV EDLAKLVVGS FQEIEHLMDE GNKARTVAAT NMNETSSRSH AVFTLMLTQK
RFDPETKMEM EKAAKISLVD LAGSERATST GATGARLKEG AEINRSLSTL GRVIAALADL
STGKKKKGSA AGQVPYRDSV LTWLLKDSLG GNSMTAMIAA ISPADINYDE TLSTLRYADS
AKRIKNHAVV NEDANARMIR ELKEELAQLR SKLGNGGVVG DTHVPGEEVY AEGTPLEKQI
VSITTPDGTV KKVSKAEIAE QLNQSEKLLQ DLNQTWEQKL QKTEEIHKER EAALEELGIS
IEKGFIGMST PKKMPHLVNL SDDPLLAECL VYNLKPGSTS VGNVESNAEH QANIRLNGSR
ILHEHCVFEN AADGTVTVIP KEGAAVMVNG KRVTEPTRLH SGYRIILGDF HIFRFNHPLE
AKAERAERAE QQSLLRQSLT ANQLQALEKS PNLSPSHNHQ QSLSTAVSEG DSSRPDSPAP
FSRNTKESDW SFARREAAGA ILGTDQNFAK LTDEELNALF EDVQRARAER VNVREGDEDI
ESMASYPTRE KYLSTGTLDN FSLDTALTMP STPKQAETEE KLGQIRDVMQ GQLDKQKEEY
KDQLKTAEAA NVEVEEIKKE KARMEETLMQ LKVDMQKQLE MQRRQFEDKI EKLDPLKRPK
ANPKLSADEI ERAKAVVKKW RSRRYVLMAE AVLQHAATLK EAQVMSHELN ESVVFQFTIV
DVGHLLCSSY DMVLNGLTGE GDDIALETAL KPCVGIRVID YKHSVVHLWS IEKLHDRVRQ
MRQMFQYLDQ PEYAQHLSLD NPFVETCMPQ YTLVGEVDVP LKTVFESRVQ DFTLDVTSPH
TSHAIGMIKL ALEPSSARAP TNTLKFNVVM HEMIGFAERE GTEVHAQLFI PGISEEDGIT
TTQMIRDFDE GPIRFESVHS MSIPLFASQD TSLRVAIFAK VSAMHLDKLL SWDDMRDAVP
TSHSKPKGAR INESHFYTEG KHDLLARVQI LELNEEGDYV PVEVTQTSEL DNGTFQLHQG
LQRRVAITVT HSSGDALPWN DATSLRVGKI ALLDSAGKTP DMGSASPPLP LRLVTEPTFR
VNANGTRSVT LIGQWDSSLH NSLLLDRITS EKYRVQMTVS WEINSEKLAE PIKFSLPVAV
QVVSRNFVRQ TSMFSSLWQN IRIVHSSTGI FTVQMRPAPI KRVGDLWRMS SQHDYVKGEE
NLGTWTPRGV SLVADYISAR KKKRMMTELT AVQGRLKKLG FGDANDLSNG VDDTGDDSDL
PPPKTNSETD SIAELLQDDP PEVPELPTPQ EGPSPEDEVA PRAETEQEEQ TNSAELNQPT
DSTKSPPEYT DAQTYLLNRC LKLWQRYPDP TAKILSPANT DPPTDGYADS ISDQKSTLEF
VASVIRVPKN PTVLKGGYLL VPNSDATKWN KRFVELRRPY LHIHSVADGE EVGIVSLRNS
RVDSQPGILG LLNDDYDTGG SGGFGGSDDG YGLLDNLNGN MDNNNRAANG RPSGLLDTIM
SGGSGGSGGR VSNSNISTPQ QRRSPSALLI SSLWPTFSPL PSPNPMTAAG ARSSHSRLAS
GGNRTSAVSL RSNTSSPASS TGTLAATTTT NNNNGPLSSS GPSLQQGGGL SRLSERLQAG
VFAIYGTDNT WLFAARSEKD KMDWIWKIDQ SYMMTSPSAS VAGSRGGSRA GSARGSRAVS
PSPGARRTSA RVSQLRF
//
