ID L8X2V7_THACA Unreviewed; 1719 AA.
AC L8X2V7;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Kinesin-like protein {ECO:0000313|EMBL:ELU43338.1};
GN ORFNames=AG1IA_02634 {ECO:0000313|EMBL:ELU43338.1};
OS Thanatephorus cucumeris (strain AG1-IA) (Rice sheath blight fungus)
OS (Rhizoctonia solani).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Ceratobasidiaceae; Rhizoctonia; Rhizoctonia solani AG-1.
OX NCBI_TaxID=983506 {ECO:0000313|EMBL:ELU43338.1, ECO:0000313|Proteomes:UP000011668};
RN [1] {ECO:0000313|EMBL:ELU43338.1, ECO:0000313|Proteomes:UP000011668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AG-1 IA {ECO:0000313|Proteomes:UP000011668};
RX PubMed=23361014; DOI=10.1038/ncomms2427;
RA Zheng A., Lin R., Xu L., Qin P., Tang C., Ai P., Zhang D., Liu Y., Sun Z.,
RA Feng H., Wang Y., Chen Y., Liang X., Fu R., Li Q., Zhang J., Yu X., Xie Z.,
RA Ding L., Guan P., Tang J., Liang Y., Wang S., Deng Q., Li S., Zhu J.,
RA Wang L., Liu H., Li P.;
RT "The evolution and pathogenic mechanisms of the rice sheath blight
RT pathogen.";
RL Nat. Commun. 4:1424-1424(2013).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ELU43338.1}.
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DR EMBL; AFRT01000576; ELU43338.1; -; Genomic_DNA.
DR STRING; 983506.L8X2V7; -.
DR HOGENOM; CLU_240327_0_0_1; -.
DR Proteomes; UP000011668; 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 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 InterPro; IPR013272; Vps72/YL1_C.
DR InterPro; IPR046757; YL1_N.
DR PANTHER; PTHR24115:SF1014; KINESIN-LIKE PROTEIN SUBITO; 1.
DR PANTHER; PTHR24115; KINESIN-RELATED; 1.
DR Pfam; PF00225; Kinesin; 2.
DR Pfam; PF05764; YL1; 1.
DR Pfam; PF08265; YL1_C; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SMART; SM00993; YL1_C; 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:UP000011668}.
FT DOMAIN 813..1277
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 26..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 719..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 950..979
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1282..1346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1442..1677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 177..205
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1370..1416
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 34..60
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..122
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..440
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..515
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 728..798
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1456..1490
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1511..1528
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1539..1553
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1554..1570
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1571..1589
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1590..1608
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 906..913
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1719 AA; 187194 MW; 6A26792CA7CFBD67 CRC64;
MSLSATRSRR SNAGNRWAEA LAAVQLENGD APDPDAEAPG EEFVGKEEED VFESDFESTD
EEEYAKQGVD DGEKQVQMEE KAERRAARAK ASKIGAAPTQ KILERAMRGE PAPKKRRIST
KNNVEKRASI YWDATRQSER SSTVKHKFLV QERLKDAENR KAHAPRRPRP IAAPKTQDEL
IAAALELEEK NTKALNEFLQ KEEEKRAAAR KVVRLKIEGP VIRWISRGEV PRIEEVKVEQ
GTNETSIVSS QAPVQPPIIQ APSTQDPVTH AVSVPVEKNS TPVLLEDSTP LVSTSTSAPV
FTPVSTPAPV STTSHASSRA STPLRTQRMQ VYVEIPTPSK SMRRSLSSSS VQGSSLALRG
REASPSPVIS RGLSAPLSQP PVRSPLSSTA SLPRSPLSTC EPLVPEIGSS KPPGSVLSQP
SRITSTQSSE TASSQLPESI LPQADPLHNL HRPTVVRQSS VGSSSSSKSK GKMIMFVEIP
VRKKERSGTP VPDSTARTEQ SSGGMVQQRS SLSDPPSYTP IPPPYLGPGP SGSSTAALTL
PARTIPSAPI THSGPTACPV QKQMRNYVVV EYGGGARASF GWNMQAMFGN HADWEDVLLH
GVKPLRKFPP SFLSNTRSLM IGLIDPVKPT CAITGLPAPY RDSRTGIPYA NAYAYKTLTR
LLAHEFIWSK ERGCYVGDEG KDPAKGVPAN WRSAASGRLQ RVVISKSLSL IQPHDTHKLY
IMPPVTRNKA PDSSSSASGT TQQQQTRATR SSAVRSPSET KSKLAATTTS SAPPPKPVGS
TLSRSTTNRM SVVLPTNKKS IGTKEKDKDD REPMRAFLRI RPAPSSANST PYIATLSETT
VEMSDPSPAA PRFGMRPSLA PAPSLTYTFT RVFPPETLQP EFFASTTLPL VKDLLSGENG
LVFAYGVTNS GKTFTIQGGN GKGEGGLLPR TLDVLFNNAK WRPAKCSSVE KEPSYGSSIK
SKNGPAVEPD VESLMGEEAA DRDDTTIKVD RNYEYSVFVS YAEIYNEKIF DLLASESLTS
ESSSMSRSGS GQSLSRSLHA KPLPKYLSAL LPKSFSSHLG FGSSSSANSM SGSTGPGGEI
PGSITRKALA LKSDPVTNGK FVSGLREIRV RSAQEGRAIL KLGQINRTVF GTVANERSSR
SHAVFTIKVL RVHKGADKED PEEVQCARLS VVDLAGSERS KNTHATGDRL KEAGNINKSL
MVLGQCMEML RANQRKISAG GTLKLGVVPF RHSKLTELFM DFFVGEGRAM IVNVNPYDTG
FDENSHVMRF SALAREVATT TQRILPPRPP PAKSSGLATA RGLSTSIGPG VGTGPAPKAG
SPAPPVRTAR KVRLSEGTPG QSESRLMVFL AEDETNDEDD DDDTPRDTLV DELFEEVEYL
RERLFEAEMR ASTIEAEIRE EVMKEMEERM QTMEKMFMRR LASEVEAGES KTDRKIDMLQ
RAGLLQSRQD SDSEDEENIE KSLMVEDETE TDDEEDEDED EDEEEDEEEP ESPTPHHKRL
TGQPLATLEE GESFEESELT DDESNESGEE PQVTMGEASM DIEDDDEIPE TEEEDQSTPS
KSRKQRVESD EEEYEQDEDE DEEEEEEEYV PTPPTKSKSR RESTSRTPKS KGKAPGNTPK
AKRDSTPSAP PPGPDQDGDE SMLAAAIVPN KRARAARLSA SGPGSTYIPA PGEPEAVKKK
KRQLGKVSAM TEDQIWAAAM KVDHEKQTMG VRRFGRGSR
//
