ID G4UH78_NEUT9 Unreviewed; 1882 AA.
AC G4UH78;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Kinesin-domain-containing protein {ECO:0000313|EMBL:EGZ75470.1};
GN ORFNames=NEUTE2DRAFT_164337 {ECO:0000313|EMBL:EGZ75470.1};
OS Neurospora tetrasperma (strain FGSC 2509 / P0656).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=510952 {ECO:0000313|EMBL:EGZ75470.1, ECO:0000313|Proteomes:UP000008513};
RN [1] {ECO:0000313|EMBL:EGZ75470.1, ECO:0000313|Proteomes:UP000008513}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain FGSC 2509 / P0656 {ECO:0000313|Proteomes:UP000008513};
RX PubMed=21750257; DOI=10.1534/genetics.111.130690;
RA Ellison C.E., Stajich J.E., Jacobson D.J., Natvig D.O., Lapidus A.,
RA Foster B., Aerts A., Riley R., Lindquist E.A., Grigoriev I.V., Taylor J.W.;
RT "Massive changes in genome architecture accompany the transition to self-
RT fertility in the filamentous fungus Neurospora tetrasperma.";
RL Genetics 189:55-69(2011).
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; GL891107; EGZ75470.1; -; Genomic_DNA.
DR STRING; 510952.G4UH78; -.
DR eggNOG; KOG0245; Eukaryota.
DR HOGENOM; CLU_001485_20_2_1; -.
DR Proteomes; UP000008513; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
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:UP000008513}.
FT DOMAIN 13..364
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT DOMAIN 1576..1841
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..1514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1667..1708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1728..1798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 766..821
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 630..667
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1485..1502
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1731..1798
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 1882 AA; 207092 MW; 9E46611BF4EA72E4 CRC64;
MAPGMAPMGG GGNIKVVVRC RPFNAREHDR GAQCIVEMRD NQTVLTPPPD 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 PNLSPSHNHH QSLSTAVSEG DSSRPDSPAP
FSRNTKESDW SFARREAAGA ILGTDQNFAK LTDEELNALF EDVQRARAER VNVREGDEDM
ESMASYPTRE KYLSTGTLDN FSLDTALTMP STPKQGETEE KLGQIRDVMQ SQLDKQKEEY
KDQLKTAEAA NVEVEEIKKE KARMEETLMQ LKVDMQKQLE MQRRQFEDKI EKLDPLKRPK
ANPKLSADEI ERAKAVVKKW RSRRYVLMAE AVLQHAATLK EAQVMSHELN ESVVFQFTIV
DVGHLLCSSY DMVLNGLTGE GDDIALETAL KPCVGIRVID YKHSVVHLWS IEKLHDRVRQ
MRQMFQYLDQ PEYAQHLSLD NPFVETCMPQ YTLVGEVDVP LKTVFESRVQ DFTLDVTSPH
TSHAIGMVKL ALEPSSARAP TNTLKFNVVM HEMIGFAERE GTEVHAQLFI PGISEEDGIT
TTQMIRDFDE GPIRFESVHS MSIPLFASQD TSLRVAIFAK VSAMHLDKLL SWDDMRDAVP
TSHSKPKGAR INESHFYTEE KHDLLARVQI MELNEEGGYV PVEVTQTSEL DNGTFQLHQG
LQRRVAITVT HSSGDALPWN DATSLRIGKI ALLDSAGKTP DMGSASPPLP LRLVTEPTFR
VNANGTRSVT LIGQWDSSLH NSLLLDRITS EKYRVQMTVS WEINSEKLAE SIKFSLPVAV
QIVSRNFVRQ TSMFSSLWQN IRIVHSSTGI FTVQMRPAPI KRVGDLWRMS SQHDYVKGEE
NLGTWTPRGV SLVADYISAR KKKRMMTELT AVQGRLKKLG FGDANDLSNG VDDTGDDSDL
PPPKTNSETD SIAELLQDDP PEVPELPTPQ EGPSPEDEAA PSAETEQEEQ TNSAEPNQPT
PDAADSNKPP PEYTDAQTYL LNRCLKLWQR YPDPTVKILS PVNTDPPTDG CADSTSDQKS
TLEFVASVIR VPKNPTVLKG GYLLVPNSDS TKWNKRFVEL RRPYLHIHSV ADGEEIGIVS
LRNSRVDSQP GILGLLNDDY GTGGSGGFGG SDDGYGLLDN LNGNMDNNNR AANGRPSGLL
DTITSGGSGG SGGRVSNSNV STPQQRRSPS ALLISSLWPT FSPLPSPNPM TAAGARSSHS
RLASGGSRTS AVSLRSNTSS PASSTGTLAT TTITNNNKNN NNGPLSSSGP SLQQGGGLSR
LSERLQAGVF AIYGTDNTWL FAARSEKDKM DWIWKIDQSY MMTSPSASVA GSRGEVERGV
QGAVGRLARV LGRGGRARGL VS
//
