ID A0A444ZG62_ARAHY Unreviewed; 804 AA.
AC A0A444ZG62;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN ORFNames=Ahy_B04g070289 {ECO:0000313|EMBL:RYR13144.1};
OS Arachis hypogaea (Peanut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Arachis.
OX NCBI_TaxID=3818 {ECO:0000313|EMBL:RYR13144.1, ECO:0000313|Proteomes:UP000289738};
RN [1] {ECO:0000313|EMBL:RYR13144.1, ECO:0000313|Proteomes:UP000289738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Fuhuasheng {ECO:0000313|Proteomes:UP000289738};
RC TISSUE=Leaves {ECO:0000313|EMBL:RYR13144.1};
RA Chen X.;
RT "Sequencing of cultivated peanut Arachis hypogaea provides insights into
RT genome evolution and oil improvement.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
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:RYR13144.1}.
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DR EMBL; SDMP01000014; RYR13144.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A444ZG62; -.
DR STRING; 3818.A0A444ZG62; -.
DR OrthoDB; 239968at2759; -.
DR Proteomes; UP000289738; Chromosome b04.
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; cd01367; KISc_KIF2_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; PTHR47971:SF1; KINESIN-LIKE PROTEIN; 1.
DR PANTHER; PTHR47971; KINESIN-RELATED PROTEIN 6; 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|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW ProRule:PRU00283};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00283,
KW ECO:0000256|RuleBase:RU000394};
KW Reference proteome {ECO:0000313|Proteomes:UP000289738}.
FT DOMAIN 200..534
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 534..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 630..683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 713..751
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 550..569
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..647
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..675
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 290..297
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 804 AA; 89331 MW; BF824801F5CDEC22 CRC64;
MQQSNAAAAA LYDGGGGSLH GAGNAATDAG DAVMARWLQS AGLQHLASPV ASTGIDHRLV
PNLLMQGYGA QSAEEKQRLF KLMRNLNFNG ESGSEPYTPT AQILGGVPLS DGPYSPDFRG
DFGAGLLDLH AMDDTELLSE EVIAESFEPS PLLPADTRAF QDDFNPVNSK QEQGEADFDA
SISLPMNELD NSTRENNVAK IKVVVRKRPL NKKELAKKED DVVSVSDYAY LTVHEPKLKV
DLTAYVEKHD FCFDAVFDEN VTNDEVYRDT VQPIIPTIFE RTKATCFAYG QTGSGKTYTM
QPLPLRAAED LVRQLHQPFY QNQKFKLWLS YFEIYGGKLF DLLGDRKKLL MREDGRQQVC
IVGLQEFEVS DVQIVREFIE KGNAARSTGS TGANEESSRS HAILQLAIKK HKEVKESKRN
NDKNEERNGK LVGKISFIDL AGSERGADTT DNDRQTRIEG AEINKSLLAL KECIRALDND
QIHIPFRGSK LTEVLRDSFV GNSKTVMISC ISPGAGSCEH TLNTLRYADR VKSLSKSGNP
RKDQPPNPAP QANKEVSSTS TSSLPAGAGS ENFYDQCQVK PMDIGRKFIE KESSLYSSAA
DVVDKQLLVN EREEKGLGSA SMDKERFEVK NSCNGSTSQS MNSYSQNDTD ERMKKVSSPY
RRRPNDTERP ANCMKRDSNG SDMFTTNSYQ QSIGNYNTIA TGSRLYEAES SPNNNISEIL
EEEEALIAAH RKEIEDTMEI VREEMKLLAE VDKPGSLIDN YVTQLSYVLS RKAASLVGLQ
ARLARFQHRL KEQEILSRKR LPRQ
//
