ID A0A3N4J0Y9_ASCIM Unreviewed; 1058 AA.
AC A0A3N4J0Y9;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 22-FEB-2023, entry version 15.
DE SubName: Full=Kinesin-domain-containing protein {ECO:0000313|EMBL:RPA87584.1};
GN ORFNames=BJ508DRAFT_320590 {ECO:0000313|EMBL:RPA87584.1};
OS Ascobolus immersus RN42.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Ascobolaceae; Ascobolus.
OX NCBI_TaxID=1160509 {ECO:0000313|EMBL:RPA87584.1, ECO:0000313|Proteomes:UP000275078};
RN [1] {ECO:0000313|EMBL:RPA87584.1, ECO:0000313|Proteomes:UP000275078}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RN42 {ECO:0000313|EMBL:RPA87584.1,
RC ECO:0000313|Proteomes:UP000275078};
RX PubMed=30420746; DOI=10.1038/s41559-018-0710-4;
RA Murat C., Payen T., Noel B., Kuo A., Morin E., Chen J., Kohler A.,
RA Krizsan K., Balestrini R., Da Silva C., Montanini B., Hainaut M.,
RA Levati E., Barry K.W., Belfiori B., Cichocki N., Clum A., Dockter R.B.,
RA Fauchery L., Guy J., Iotti M., Le Tacon F., Lindquist E.A., Lipzen A.,
RA Malagnac F., Mello A., Molinier V., Miyauchi S., Poulain J., Riccioni C.,
RA Rubini A., Sitrit Y., Splivallo R., Traeger S., Wang M., Zifcakova L.,
RA Wipf D., Zambonelli A., Paolocci F., Nowrousian M., Ottonello S.,
RA Baldrian P., Spatafora J.W., Henrissat B., Nagy L.G., Aury J.M.,
RA Wincker P., Grigoriev I.V., Bonfante P., Martin F.M.;
RT "Pezizomycetes genomes reveal the molecular basis of ectomycorrhizal
RT truffle lifestyle.";
RL Nat. Ecol. Evol. 2:1956-1965(2018).
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; ML119646; RPA87584.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N4J0Y9; -.
DR STRING; 1160509.A0A3N4J0Y9; -.
DR Proteomes; UP000275078; Unassembled WGS sequence.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
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; cd01370; KISc_KIP3_like; 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; PTHR47968; CENTROMERE PROTEIN E; 1.
DR PANTHER; PTHR47968:SF13; 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:UP000275078}.
FT DOMAIN 10..381
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 641..908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 958..996
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1037..1058
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 396..459
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 644..674
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..716
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 775..839
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 851..873
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 958..972
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1040..1058
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 137..144
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1058 AA; 115732 MW; EB7A1635EEB9146A CRC64;
MEDLDSGASS ISVTVRVRPF TIREAAQIPR CDDSPAFFGD GSLAATPQPK ITSKGIRKVI
KVIDDRVLVF DPPEDNPLAR FGKQILGPQG KRVKDMRFGF DKIFDEDATQ EEVYQATSQK
LLDNVLDGFN ATVFAYGATG CGKTHTISGT KQHPGIIFLT MRELYEKMDA LKHDKDIELT
LSYLEIYNET IRDLLVPGGS KQGLALREDA NKTIAVAGLS THKPAGVDEV MDMILEGNAN
RTVSPTDANA VSSRSHAVLQ INISQRDRTA GLSENHMFST LSIIDLAGSE RASVTKNRGD
RLLEGANINR SLLALGNCIN ALCENKKGNH IPYRDSKLTR LLKFSLGGNC KTVMIVCVSP
SSQHYDETHN TLKYADRAKK IKTKVSRNMM NVDRHVSQYV KAIFDLRQEV EDLKRRLGDS
TKDAMVKVQK TQNNRDLALR EASRRIKVAH EQSKEARNTR IQDMKSLRLM EKRANVVASW
IAAFDQVFAS RQDEAQLAGV FSVRMAADQV LMELQSNRNM LQQRLSSSNP EKAYDNTVSQ
MLEHLRGVEG VTDMDISAFK NEAQMLSVTA DRDMYQALAE YDSESTNSVQ SLTKAHFESV
ATINKLITVE GEDAMEVDQD ALRILMQSCV DATSHVVKPS GELVSTEGLT SAPSGTPRRK
KSFTQTQQDF QAPPASAFQP PVSFIPNPSS PVKNSPRRFR VRTPRKAGGA AQRRKEKKKV
RWQDEETDEP LGESMPTPVR YREPPPSQSL PSQSSQPGLM GPPPRRPNFG PQLDGHQSAP
DQSEGSASFQ GQASALQPQP QATLPSSPVQ QAARRPQQSN ENLEHPGDTS ISHITKNRHL
QAGFLSRKSG GRGSGSPTDS ATTRRQSLSA FQPLQEFDEH RLLQKSNSNY DGLGDTSMSM
NPPAPVYEGV KPSFRASISR DSAIHKHRAP RSSLGGGSLS SASAIRARRA SLAPLASIGE
SGNGSAQFKK PALPSGNPTR RMSLARMGPP SDVGNSSMNR IAPIKSHNRR LTVSGIGSGG
VKLNPAALQM ALATAGVDPN DANSRANSSF SLNKPVWR
//