ID M7BQ82_CHEMY Unreviewed; 1543 AA.
AC M7BQ82;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Kinesin-like protein KIF14 {ECO:0000313|EMBL:EMP40086.1};
GN ORFNames=UY3_02662 {ECO:0000313|EMBL:EMP40086.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP40086.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
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; KB514586; EMP40086.1; -; Genomic_DNA.
DR STRING; 8469.M7BQ82; -.
DR eggNOG; KOG0245; Eukaryota.
DR Proteomes; UP000031443; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; 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; cd01365; KISc_KIF1A_KIF1B; 1.
DR Gene3D; 1.10.287.3160; -; 1.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR InterPro; IPR000253; FHA_dom.
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 InterPro; IPR008984; SMAD_FHA_dom_sf.
DR PANTHER; PTHR47117:SF3; KINESIN FAMILY MEMBER 14-LIKE; 1.
DR PANTHER; PTHR47117; STAR-RELATED LIPID TRANSFER PROTEIN 9; 1.
DR Pfam; PF00498; FHA; 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; SSF49879; SMAD/FHA domain; 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|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00283};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00283}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000031443}.
FT DOMAIN 371..715
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 15..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 726..775
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 860..1002
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 298..332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 460..467
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1543 AA; 173088 MW; AA88C8D5919706D3 CRC64;
MPIYTVPTRN HTDVLGVSSF QKNPPQNTFP KSNRFGQQLK SQGPENEKDN SLSLTKTKEI
NRTYVISACK NAGDTSVTFK PEGRLTLQRR TGASKISTSI DKQLEENTAQ DVENTQTNGR
LTLQRRMGTG SIEKHKTNKN REPGIENSDS VVAQTNNKNV FPPGISTNNT HYIKSSTQLV
EGQMNGKRCS DLKNKDSLAN LNGSSGNENS KCLKYRTTIA DAKIQNDVPR SAHLIATKLV
NRTPGVKLNE KDNFNELTGK ERIRNSVAKY GSLERQRTPR NGGPTEGIKA TPMRGTLQDA
KSPASSTLKN RTPCLQVTQK KNTNASNSLS ISRSARAEES QIFMQPAALK IETVAQNTCT
DENPLKVENS KVTVAVRVRP FSDRERKEKA SQVVSMSGQE TVVRHPETKQ VYNFIYDFSF
WSFDHCHPNF ASQNTIYKAL AVPLLERAFE GYNTCLFAYG QTGSGKSYTM MGFGEELGII
PRFCEDLFTQ IAQMDTQQIL YHFEMSYFEV YNEKIHDLLI FKAENGQKKQ PLRVREHPVL
GPYVEDLTAN MVSSYSDIQS WLELGNKQRA TAATGMNDKS SRSHSVFSLV MTQTKTEFVE
GEEHDHRITS RINLIDLAGS ERCSPTQTSE ERLKEGVSIN KSLLTLGKVI SALSEQSQNR
KRAFIPYRES VLTWLLKESL GGNSKTTMIA TVSPAASNVE ETLSTLRYAK QARLIINTAK
VNEDVNAKLI RELKAEIEKL KAARKSALNT DPEKYRQYLQ EITSLRVKLH QQERDMAEMQ
SVIKNVDGRV SITPLGEAKT YVNGKHISEP TVMHHGDRVI LGGDHYFRFN HPVEVQKVKK
PSCGTTLSCD GPKDFEFAKN ELLVAQRSQL ESEIEEARLK AKEEMMQGIQ VAKEMAQQEL
ISQKKVYESK IKSLEAELRE ESHKKQIQEM NNQQTTNKIQ ELEKAKQHLE LEVHFSKKRL
EMETFATRQA LEDHTIRHAK ILEALEAEKQ KIAKEIETLQ QNRGNGNKTI TIKPNWNSMK
LSLMIQEANT ISSKLGKHTV FCRHDISEEG NGTGPSVKVL VRNLKLEIAT FWSLEKFEYK
LAAMKELYES NGSNKADVFY DPADEWEPDL TTTSISSFSR RRSRSLMKNR RISGCLSDIK
LQPIQGLHTS HLSGSVNKSG SICSSSSESF LPGICKELIG SALDLLGQNH EEEKSIADSL
LSNLLTIYTG VTAISNAYEQ QDEESQENFF SLDRATQSCS IRITSAFEQL VVLTKHWLNS
FQKCTDSLKI DEELRQGVKN LGGYLQLLLQ GCCSDISSMV TEAHNKIIQI VKQAGKHVGH
LTALIGSDLH LSEDTKEDAT ISQEDFILAI YDGVGSGLKS LLDSVQKKTR EMQKELLKQY
QQNEIQNQIK NNAVAFARCL ENTISECKKF MELLPEDSMA AFSALVVERR LVARASLQAV
LDVANSATWT MASAVAMRRS SWLQASGLPY EVQQTISEKM DLWLRSLKDS RATLSSLDLH
TLARTILSPR LDSTNLRIGR TILKCIIETT GGGLLLHLRA LGR
//
