ID A0A1E1KEH3_9HELO Unreviewed; 1745 AA.
AC A0A1E1KEH3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Related to kinesin-like protein {ECO:0000313|EMBL:CZS96453.1};
GN ORFNames=RCO7_04869 {ECO:0000313|EMBL:CZS96453.1};
OS Rhynchosporium commune.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Ploettnerulaceae; Rhynchosporium.
OX NCBI_TaxID=914237 {ECO:0000313|EMBL:CZS96453.1, ECO:0000313|Proteomes:UP000178129};
RN [1] {ECO:0000313|EMBL:CZS96453.1, ECO:0000313|Proteomes:UP000178129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UK7 {ECO:0000313|EMBL:CZS96453.1,
RC ECO:0000313|Proteomes:UP000178129};
RA Ploux O.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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; FJUW01000012; CZS96453.1; -; Genomic_DNA.
DR STRING; 914237.A0A1E1KEH3; -.
DR InParanoid; A0A1E1KEH3; -.
DR OrthoDB; 1430657at2759; -.
DR Proteomes; UP000178129; 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; 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:SF15; ZGC:66125; 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:UP000178129}.
FT DOMAIN 52..439
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 472..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 723..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 865..886
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 902..947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1555..1628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1691..1717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 670..704
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 953..998
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1238..1265
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1341..1410
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1459..1553
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 25..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 723..744
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 768..792
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 902..925
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1591..1624
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 139..146
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1745 AA; 194438 MW; 9770BC56FCA71429 CRC64;
MASSPPESPL AGPQRPVSAM MRPPPRTTSR MSMTSKAGGS GSRASDEDGK TAVRVAVRIR
PSLKSTDPGF DLIPQRFQRS MVQVTSPTSL AIDSPQGRKL FVFDRVFSED VSQEGVWDYL
VESTNAFVQG YNVSMMAYGQ SGAGKSYTMG TSGPEQQADM EYMGVIPRAA IALFDKLEGL
RNSSRNSMSG LRTPTRYSTT AAAILAKNME KTWTLKATYV EIYNESLRDL LVPEGVPYSE
RGNVTIREDT KGHILLTGLH QVDINSVEDL LAALNFGSMI RQTDSTAINA KSSRSHAVFS
LNMVQRKSKL QTQGAEKRFS VPLEAMTGAD TMVTIESKFH FVDLAGSERL KNTGAQGERA
KEGISINAGL ASLGKVISQL SSRQAGSHVS YRDSKLTRLL QDSLGGNAIT YMIACVTPAE
FHLSETLNTV QYAQRARAIQ SKPRIQQVSD ETDKQALIER LKAEVAFLRE QIRSTERSGD
RRPHATTERP ERQNEREVEL QNQLLDVQEG YTTLSQRHAK LISEMAKARD SELADNQAFE
NTLGDSATER LKRSNSFAEA VEQVVLEYEK TIQTLEQSLS STRGSLSNTE TILLEKENKC
AYVETVNSQL QARLQKLIDR ESSTENYLHD LEAKLDGHTS GEEKNSAIVL ELRKEIARVR
ENEAACEDYI STLEERLAEA DQDAELMQRE IDRLEHVVER QRSLGKLDNL LYELDHIQQD
GNSVVAESPL TNGKRQSYEH SRQQSFTSRR SHKDVILETE EGEEDDLSPT STTEKAHRTE
SEGPDDSGEP IDRDPVPVLL EPATNEYPPQ SPAQSKFVED KLENVSQELF DLRVEHESTV
NEFDNLSRKY EEALRTLAEL QDAVDEARHP SNNRDSTFSI SSPTDTANAS FLTDARVNEL
KDGGQYSSSR SLSSELSSAG ELPSTMESSD AEAAIKKSES GEVARGSANG ETIAVEVDNL
RKLAAEKEQA QQLLAEKYAQ LEEKHMETLD FVEELKAEVS KAKMVEASST PRSVTPVIRR
KSSQNVMIID KAHRAFASLR NIGTESFEHS PDIMANFELN LNTAMHELHS RSERVQELEH
DITAVKKEME TKMAIISGLT RERSSMKASP MDMSVVSTMR DQLLQSENQM RLLQDTHASR
EQELKAELEN LRVSMEAHAT SFKDDKALGE RVLGESNAHK EIQEKKIATL EMKLAEWEGR
HETALKSMQS SEKGLLDTIA GLEQQLTSLK TGQQTKDLDS ENEAVKNLQR EVDEHKATVA
ANAARVAELE QSHATTRQQL DEITRGRDTS NAELEGHKVL ISRLEQQIAE HEIIVKTHQD
GMNLLQANHA KDLEVLKSST HEDYEARYSE IRSEYQAKME EIQSELAEAR DNLTKIATQV
AFALGVDVST DKLEERIADL LADQKALAEE TKKGSEREKI VLELSGINDT VMKELQSVKV
ELAELLIQTA EGAKFKNDHA TVAEQLAALR KEMTDLETKN KKNSRLVEEL EDQLASNFDQ
HQIANNRFST LQTERNAQVD EANAAHLRTQ AELDAIKEEY ASLQAKLEDV QLAQVGPAPT
RPDSAASQLH KTASVASLPS PPPAIPLPPL PGSNNASNSA NGHAASIPVP QTPTLGNRPS
SKDLATSQIH EDQEARIRTI EKHLHAEKQL TQTLEEALTD LERQSNKMKA EVDAWKRRAA
DLELELKEAK EREKNGGLDK ENRWSMQQVE EERKKRRDAE IARAHLEERM NAISKKKKKG
SLNCF
//
