ID A0A367KXR4_RHIST Unreviewed; 902 AA.
AC A0A367KXR4;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN ORFNames=CU098_001834 {ECO:0000313|EMBL:RCI06975.1};
OS Rhizopus stolonifer (Rhizopus nigricans).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX NCBI_TaxID=4846 {ECO:0000313|EMBL:RCI06975.1, ECO:0000313|Proteomes:UP000253551};
RN [1] {ECO:0000313|EMBL:RCI06975.1, ECO:0000313|Proteomes:UP000253551}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LSU 92-RS-03 {ECO:0000313|EMBL:RCI06975.1,
RC ECO:0000313|Proteomes:UP000253551};
RX PubMed=29674435; DOI=10.1534/g3.118.200235;
RA Gryganskyi A.P., Golan J., Dolatabadi S., Mondo S., Robb S., Idnurm A.,
RA Muszewska A., Steczkiewicz K., Masonjones S., Liao H.L., Gajdeczka M.T.,
RA Anike F., Vuek A., Anishchenko I.M., Voigt K., de Hoog G.S., Smith M.E.,
RA Heitman J., Vilgalys R., Stajich J.E.;
RT "Phylogenetic and Phylogenomic Definition of Rhizopus Species.";
RL G3 (Bethesda) 8:2007-2018(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,
CC ECO:0000256|RuleBase:RU000394}.
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:RCI06975.1}.
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DR EMBL; PJQM01000051; RCI06975.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A367KXR4; -.
DR STRING; 4846.A0A367KXR4; -.
DR EnsemblFungi; RCI06975; RCI06975; CU098_001834.
DR Proteomes; UP000253551; Unassembled WGS sequence.
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; cd01369; KISc_KHC_KIF5; 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:SF29; 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 ECO:0000256|RuleBase:RU000394}; Coiled coil {ECO:0000256|SAM:Coils};
KW Microtubule {ECO:0000256|RuleBase:RU000394};
KW Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283,
KW ECO:0000256|RuleBase:RU000394};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00283,
KW ECO:0000256|RuleBase:RU000394};
KW Reference proteome {ECO:0000313|Proteomes:UP000253551}.
FT DOMAIN 5..328
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 847..902
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 419..513
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 573..614
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 648..692
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 86..93
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 902 AA; 101513 MW; 1C1FE190AED6A153 CRC64;
MSGNNIKVVC RFRPQNKLEI KEGGVPIIEI EDDGTQLSLK GETTSNYAFD KVFGSHTPQQ
DVFEYSIKSI VDDVTAGYNG TVFAYGQTGS GKTYTMMGSD IDDENSKGII PRIVEQIFTS
INDSPSNIEF TVKVSYMEIY MERVKDLFNP SNDNLAIHED KARGVYVKDL YEIYVANRDE
VYTAMKNGGS NRVVAYTNMN AESSRSHSIV VITITQKNLD TGAAKSGKLY LVDLAGSEKV
GKTGASGQTL EEAKKINKSL TALGMVINSL TDGKSSHVPY RDSKLTRILQ ESLGGNTRTT
LIINCSPSSY NEAETISTLR FGMRAKSIKN KAKVNSDLSP AELKALLKKA KTETVTFQTY
IAALEGEVSA WRGGNTLPSD KWVTLDKINK GDFAALPPAF KSSAIMEDSR PNTPSETELT
NREKLLESLR EEMNYYKEQE SNVTNENQQM ATELSELRLQ LQKISFESKE NAINMDSLKE
ANQELQNELE ELKKNLQEVR LTYKDNADNQ KEKKKAEKIA QMMNNLDASS EINQKERQIR
ESVTKIETDG SASLSIDEVV ALRRDLADSQ ILLDQHAKTI DGLQDEKQTL ETKKVELDER
FKKLEHDYEE LLDKTIAEEE ITAQKNADIE ETIDTVKTKL EIQYASKKET HQQEIEDIKK
DIDAKSEVIL KLSQAMQSLK EANDKLHDAL NEQSTSQNSS CTEREQEIER MRKAMAKDLA
DFETMKKALM RDLQVRCEKV VELEMSLDET REQYNNVLRA SNNKAQQQKM AILERNLEQL
RNVQKQLVDQ NSSLKKEVTV SERKLNARNE RIQNLETMLL DAQDKLAKQN SKFENQLKAA
KERLEQAMSQ KSQNSMPANF GRVAKPLRGG GAAPVDGQES VPASPAERNK RTSWIAGFIS
SR
//
