ID A0A369JJL4_HYPMA Unreviewed; 2046 AA.
AC A0A369JJL4;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Kinesin motor domain-containing protein {ECO:0000259|PROSITE:PS50067};
GN ORFNames=Hypma_011769 {ECO:0000313|EMBL:RDB21522.1};
OS Hypsizygus marmoreus (White beech mushroom) (Agaricus marmoreus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Tricholomatineae; Lyophyllaceae; Hypsizygus.
OX NCBI_TaxID=39966 {ECO:0000313|EMBL:RDB21522.1, ECO:0000313|Proteomes:UP000076154};
RN [1] {ECO:0000313|EMBL:RDB21522.1, ECO:0000313|Proteomes:UP000076154}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=51987-8 {ECO:0000313|EMBL:RDB21522.1,
RC ECO:0000313|Proteomes:UP000076154};
RA Choi I.-G., Min B., Kim J.-G., Kim S., Oh Y.-L., Kong W.-S., Park H.,
RA Jeong J., Song E.-S.;
RT "Whole genome sequencing of Hypsizygus marmoreus.";
RL Submitted (APR-2018) 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}.
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:RDB21522.1}.
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DR EMBL; LUEZ02000055; RDB21522.1; -; Genomic_DNA.
DR STRING; 39966.A0A369JJL4; -.
DR InParanoid; A0A369JJL4; -.
DR OrthoDB; 1430657at2759; -.
DR Proteomes; UP000076154; 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; 2.
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:UP000076154}.
FT DOMAIN 13..463
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 51..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 792..833
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 885..920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 940..989
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1807..1902
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2009..2046
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 516..550
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 577..653
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 696..772
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1014..1055
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1238..1265
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1289..1364
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1714..1793
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1913..1940
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 289..315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 794..822
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1836..1856
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1857..1896
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 117..124
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 2046 AA; 226118 MW; 661EDDBD42F62280 CRC64;
MAPSSSSSAA TTSVQVALRI RPPTNQDSTS IPARFQRPVI HATSSTSVAI EASSNVSGSG
APNPPSVASG SAPKKQVFTF DQVHPPPTTQ YDLFTSTAKP LVSRFVEGFN CTILAYGQTS
SGKTFTMTGI DLDADPMDPN NGMGIIPRAV STIFSSAKQL KGERGGAWNY SIKGSFIELY
NEDLIDLLSL DDIGGKREVQ IREDKDGHII WGGLREVNVR NAGEVMTLLR KGTSIRRTNE
TDMNAQSSRS HAIFSLTLTQ KKYTGSTPPP RSSSPLPPGG RSPSRLARPG SMYSVTPSGS
ATRVSSPTFG RPSTPSFVSA IGRGGGLRPA SALGHAGERS QGGAEEDGGE WVTIVSKFHF
VDLAGSERLK RTAAAGERIK EGISINSGLL ALGNVISALG DPARSKSHTA THVPYRDSKL
TRLLQDSLGG NAHTLMIACV SPAEYNANET INTLKYANRA RNIKNRAVLN EREDGWDDVE
WLQGTITRLR KELKLIKDGG MVSTHESTPE VLEGAGKKVL AQMTDLQNNY EDLRSKFVER
TEELTRLRRE LGEKQRGSTA GAVGGTARYE EIVGPVIEEY EKTIGAMEAE LNLNRAALRH
TNEMVEEKED ELAAITERHA ATELYVEELR ARVAKLTERE ASTEAYVRDL EEKIKTYDES
SVTSSESLTD LKREVSRFKD AESSSAKYIT DLEARLGRAD ESVLALQQTV EKLENECDRR
RDEVGMLQSR LETLRQDGES WRTDLEERER RVKELELKMV EWEKRKKEAS DARIRLGSVV
GEVASARRSL GVNMAGTPGT SSGSEESIPP SPLTETPVDG LPSSNPAQPP HDPALENQFI
ALQQTHTATL ADLSSVTAKY RDALREISDL AAQIQEAKLS NISIAESSRA ESPSMEKPVD
IPPYRRRITG GRVRDASDPQ LNASGRRLFF RQAASAESLH GRSLSQSQSL SQELSSVHSR
KTSFSSHGTG SSHSPSNSHS HSATTSSYLT GARPNLSISL PSLSPPVNPN ERSVGSLEKE
IMRLQEVLKD REAEITLLEE SLKQSQEEKA AAAALSVSTP IENGLPNGKV TSPEPALSPK
TINQFDHIRK TMENGNGHAY HDSASEVNGS SVFSETDESL ERLNELMLSM AQKESNHREI
VDNLNSQLTH VQRQLDDLTT LSRDQALNMS TEIEGLRGKH SEDLAMLEEV QNRETALLQA
LKDAEATHAA EVEHLRIQHR QALDSKGAEV DQLIASVKQE HEASLATLRD ELATASAALE
KAHHEHEERF GASKVEQQAE IARRVQDAND ALIRSRDEHE KVLAKAKSEH VEVLKQKDAE
ATAVLQRTEE EYYNALTKVR GDHAEALKKN TAELNATLER LREEHAGELR MAEIAREGSL
SESHSSQAIV VQELQDAHAA AVTRKEASFA EEVESLKADH ARNLTTKDED YTLRMDRLRL
EYESTVAKLK EEWRVEVERL NSTLTDAHDE STATALKAQT DLDAAVRVVK EQQALVFQEY
ERGHEVEVAK LNKAHEATLQ NALTAAEEQR ASLVRSHTEA TLKLKTQHQQ EIADINNTLV
ALQEEHRERM ELTREQNERV LGEENARLSE SLAALQDDHR RDTESLRAQN ELLLSEERDR
HAAAMSGLKD EHRQALSAIQ GKNDALVKEK SNLTISLADL TKQHSQEIET LRAEHDVILQ
ELDSHKVAAD EYTLIREQTR QLHERAIGQK ADALNGMERE LRSVSGERDE LEAEVARLRG
ELDKTRGEQH KLIQEASKRD SLVGELERHR SVLAELQENL QRVKDEKDAI QVEKNRADSI
VRDLQAQIAR SASPPNVRPV PDRNMSYTRA TGLPAMKLPP PTPPPSVPPP PAPRTPGTAT
GDSNFSTSSQ GSAINSSISS RESQLDSPST SIGHMPLPPH SAQVVDPKVT VKLEQQAKQL
EEQEAMIKTL NKQLTHCESD LQTHMDLVST LETSLGDSEK NLRKARMHAT ELARERDMLN
TKIESLRNEL SEAKREVVSV RRSIVEEKQS LEQKLDEERK AKERARQQLD SRMEELQKRK
SKFACL
//
