ID K0R493_THAOC Unreviewed; 2316 AA.
AC K0R493;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Kinesin motor domain-containing protein {ECO:0000259|PROSITE:PS50067};
GN ORFNames=THAOC_34878 {ECO:0000313|EMBL:EJK46449.1};
OS Thalassiosira oceanica (Marine diatom).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC Coscinodiscophyceae; Thalassiosirophycidae; Thalassiosirales;
OC Thalassiosiraceae; Thalassiosira.
OX NCBI_TaxID=159749 {ECO:0000313|EMBL:EJK46449.1, ECO:0000313|Proteomes:UP000266841};
RN [1] {ECO:0000313|EMBL:EJK46449.1, ECO:0000313|Proteomes:UP000266841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1005 {ECO:0000313|EMBL:EJK46449.1,
RC ECO:0000313|Proteomes:UP000266841};
RX PubMed=22835381; DOI=10.1186/gb-2012-13-7-r66;
RA Lommer M., Specht M., Roy A.S., Kraemer L., Andreson R., Gutowska M.A.,
RA Wolf J., Bergner S.V., Schilhabel M.B., Klostermeier U.C., Beiko R.G.,
RA Rosenstiel P., Hippler M., Laroche J.;
RT "Genome and low-iron response of an oceanic diatom adapted to chronic iron
RT limitation.";
RL Genome Biol. 13:R66-R66(2012).
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:EJK46449.1}.
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DR EMBL; AGNL01047746; EJK46449.1; -; Genomic_DNA.
DR EnsemblProtists; EJK46449; EJK46449; THAOC_34878.
DR eggNOG; KOG0242; Eukaryota.
DR OMA; YEQHETL; -.
DR Proteomes; UP000266841; Unassembled WGS sequence.
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; -; 3.
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; PTHR47968; CENTROMERE PROTEIN E; 1.
DR PANTHER; PTHR47968:SF36; CENTROMERE-ASSOCIATED PROTEIN E; 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 SUPFAM; SSF57997; Tropomyosin; 2.
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:UP000266841}.
FT DOMAIN 88..454
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 54..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 312..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1512..1537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2214..2233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2238..2316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 463..520
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 639..666
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 812..910
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 967..1093
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1140..1174
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1203..1237
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1558..1682
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1718..1866
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1898..1951
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1978..2019
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2063..2185
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 10..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1521..1535
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2242..2265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2280..2294
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 177..184
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 2316 AA; 254388 MW; 570FD5BCE7793EC4 CRC64;
MPPAGQHKGR EEQSTLSLSN PYRRRVVSYQ AGGKPTAENR PLALGLHLPT TVLARGGTRE
MKTTPTPSKA EETTGGGGPD GKNKNEEGIL VAIRMRPLND RESQNTRVWK VLQKHSGVAQ
CTAEGKPVPG RQAGQNFFRY DRVFGERSTT GQVYSETSGE IVGGVCGGLN GTIFAYGQTS
SGKTFTMQGS GSIEDGAAPA SSLEGGGIVH MAARDIFGHI EKDPMRVFLV RVAFIEIYNE
EVRDLLVTGG GKSTLTIRED KRRGVFVDSN ETIVTSSENL LGVLFAGEKN RSVGSTAMNE
RSSRSHTIFR ITVESRIREE EPAGGDGDGS DDSDGEDDGR GDGPGTEDGA VRISTLNLVD
LAGSESVRHT GATGDRQKEG GKINQSLLTL SRVIEGLGKG AAHVNFRDSK LTRILQPSLS
GNARMAVICC TTPSELYLEE TRSTLKFAEG CKLVKTCAQV NEIMDDRSLI KKLQRELREA
RRGGPDKEAM EQMRALEEKA QVAEVANRKA EEDLKRMKDL ILKGGVLPAG DASTAAAAAA
PASSSLFVYN GADETMQLGS ETITLGTSAR GRKRRFSDGV INENDPADQL QFASPDRAGN
VKLQQARTEV KPKKVKPTAR LLPSDLKDDV DISLLRDALS AKAAQADALK ARLRDAQGRA
QAAADKLKSE HGERELLRLA KEDLESQVAL LASDKEYALS EQELIMEEKD SFISSSLEKI
EVMLEERSQQ AQAVAELQSL VESLRGQLGE AERNRTSQVD ELKVQLSSSQ EEAAAKVSEL
EGKVESSQGT ICQMTGQISL LEGESAEKTK QLDEKESALT EAQSALTSLQ ESHEVEATSL
RDRIASLEQE STRIAAEKDD ALDEAMARVS SLQDQVATLQ GAYETKDAEL QETQSTIAKL
NEDLSSSSAR TTVLEEELVS AQSASAQAAS LSDEALADAR TRIETLADEK TAISNHADGL
LVKVESLEKS NQAMTDLLSE RESALAEAQS SIEALTRDAS SQSSQLAMEA AGLRKSFESA
TEDAARLTKD LDDATKLNVD LQTQITELQG SHKNFVASLE ESSKSVAIAT SEKNGAEEKL
ATLQSRYDEL ESSSVEEVEA LKRQLANVEV ASGRKDQQVE ELSVNLAASS ARVGELEPKV
SALEDDLSSA HERVKEYSQK ITDLESTVSD SNAKFDSMDT QLNEIQREYD ASNETTRVLS
KEKEELTMKL NAAEIAKAEA NSRAEAAGDE SARLSKEISS HMETVNQLTS EVESFKSQLG
SVTTELGETV SKLDVALATV ESTTNERDTA NKRITELMSG NSNAEEVLET LQCERDELSR
NLEGAKVKLM AAEAEATSLK NEKEKLRTQL DNSLAKDEAA TSKAEEMQFQ VQEFSEKIES
LESQCEIAEQ TVRQKTEEIM ALNNAITAGN AEITNLQSQI RAVTTLNEDH QVTAKQLQNQ
VTDLEERNAQ LAKDAEELGS ELTNAQQDAS KGHQALEKEL EDCVLQLDNV SEENEAMKTK
LTALEMSISE KSKEIESLSE QLSAHESTTP APNQGDVDSL AREITDLKSL LSSANASVDE
ARSAAIASEK ELEEKEMQLE QANHALAEQE EQLRLAQEKV LLAESSHANS PHADSEELLR
EMELLMEEKN DAESRLEQEI NRRSETEANI KRTAEDERQQ LIEEAEQKME SLREEIRQLK
SDICRVESDC FDANSENTDM KDIISRLEAK ASDSESMATS ISDELKREQL DKKELQERLN
QLEEDSELFK QQVFAAKDTF EAEAKARLDE AEGRYNEAEE QRDRVERELK RSKEMIENLT
GDIEEYKAQL QRAHDLPNND TEMGLSRARE QLAQTKLLCS QSEAECLSLR QELESAKDKI
DRIKQYEHDK VSAVLPMFWS SMCIFLTSFC FFQQQKFAAK ARDAIETLKQ RLAQAESKAT
SADANALQAE VDSLVQTISE KDERIKKLEK SKITKSQIQN IQKLKLEELE AAKPSSRRSG
LRERRDDASQ HVEQLQDELK QCEIKLRKYV AHSERLEQDR NVVLEVISSC KNLPGDVVGN
SIGEMVTSIC DRLVSVEEEC DALATSETKA SEYLAELDSL RAKHSALECQ IESQTENDSG
LAESLEKSKS SLNRANDKIK QLTKDKELLK SMAESTKCSM NELQTEKRRQ MQYLESENLQ
LGEELKKAKK ELAETRVSLD AAQNGAFSGG DHTEDLQGLS SFFNSSTKRP SAIKSSCKAA
MAPATKRVPL GSARRRLESP LANQDSENLL NKSQQALSSS ALSPVATAKK KRPNPFSSIK
KARKQMTNLA RDSPTKQFVL GDTEPTADVT SECNQS
//
