ID L8IEL4_9CETA Unreviewed; 1777 AA.
AC L8IEL4;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Kinesin-like protein KIF13A {ECO:0000313|EMBL:ELR54628.1};
DE Flags: Fragment;
GN ORFNames=M91_19348 {ECO:0000313|EMBL:ELR54628.1};
OS Bos mutus (wild yak).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=72004 {ECO:0000313|EMBL:ELR54628.1, ECO:0000313|Proteomes:UP000011080};
RN [1] {ECO:0000313|EMBL:ELR54628.1, ECO:0000313|Proteomes:UP000011080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=yakQH1 {ECO:0000313|Proteomes:UP000011080};
RX PubMed=22751099; DOI=10.1038/ng.2343;
RA Qiu Q., Zhang G., Ma T., Qian W., Wang J., Ye Z., Cao C., Hu Q., Kim J.,
RA Larkin D.M., Auvil L., Capitanu B., Ma J., Lewin H.A., Qian X., Lang Y.,
RA Zhou R., Wang L., Wang K., Xia J., Liao S., Pan S., Lu X., Hou H., Wang Y.,
RA Zang X., Yin Y., Ma H., Zhang J., Wang Z., Zhang Y., Zhang D., Yonezawa T.,
RA Hasegawa M., Zhong Y., Liu W., Zhang Y., Huang Z., Zhang S., Long R.,
RA Yang H., Wang J., Lenstra J.A., Cooper D.N., Wu Y., Wang J., Shi P.,
RA Wang J., Liu J.;
RT "The yak genome and adaptation to life at high altitude.";
RL Nat. Genet. 44:946-949(2012).
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; JH881386; ELR54628.1; -; Genomic_DNA.
DR STRING; 72004.ENSBMUP00000016681; -.
DR Proteomes; UP000011080; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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; cd22729; FHA_KIF13A; 1.
DR CDD; cd01365; KISc_KIF1A_KIF1B; 1.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 6.10.250.2520; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR022164; Kinesin-like.
DR InterPro; IPR022140; Kinesin-like_KIF1-typ.
DR InterPro; IPR032405; Kinesin_assoc.
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; PF12473; DUF3694; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF12423; KIF1B; 1.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF16183; Kinesin_assoc; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00283}; Reference proteome {ECO:0000313|Proteomes:UP000011080}.
FT DOMAIN 1..300
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 504..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 591..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1341..1412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1454..1500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1574..1611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1712..1764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 312..357
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1064..1091
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 504..519
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..614
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1341..1360
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1377..1391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1454..1481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1482..1500
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1716..1759
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 50..57
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ELR54628.1"
FT NON_TER 1777
FT /evidence="ECO:0000313|EMBL:ELR54628.1"
SQ SEQUENCE 1777 AA; 198751 MW; 63AB7CAD509C191E CRC64;
QVFAFDYCFW SMDESNTTKY AGQEVVFKCL GEGILEKAFQ GYNACIFAYG QTGSGKSFSM
MGNAEQRGLI PRLCCALFQR ISLEQNESQT FKVEVSYMEI YNEKVRDLLD PKGSRQSLKV
REHKVLGPYV DGLSQLAVTS FEDIESLMSE GNKSRTVAAT NMNEESSRSH AVFNIVITQT
LYDLQSGNSG EKVSKVSLVD LAGSERVSKT GAAGERLKEG SNINKSLTTL GLVISSLADQ
AAGKGKNKFV PYRDSVLTWL LKDNLGGNSQ TSMIATISPA ADNYEETLST LRYADRAKRI
VNHAVVNEDP NAKVIRELRE EVEKLREQLS QAEAMKAPEL KEKLEESEKL IKELTVTWEE
KLRKTEEIAQ ERQRQLESMG ISLETSGIKV GDDKCYLVNL NADPALNELL VYYLKDHTRV
GADTSQDIQL FGIGIQPEHC EIDIGSDGEV SLTPKENARS CVNGTLVCST TQLWHGDRIL
WGNNHFFRIN LPKRKRRDWL KDFEKETGPP EHDLDAASEA SSEPDYNYEF AQMEVIMKTL
NSNGPLAFSL GLPDPVQNVV QVLEKQYLEE KRSALEEQRL MYERELEQLR QQLSPERQPQ
ISGPDRLAYS SQTAQQKVTQ WAEERDELFR QSLAKLREQL VKANTLVREA NFLAEEMSKL
TDYQVTLQIP AANLSANRKR GAIVSEPAIQ VRRKGKSTQV WTIEKLENKL IDMRDLYQEW
KEKIPEAKRL CGKRGDPFYE AQENHNLIGV ANVFLECLFC DVKLQYAVPI ISQQGEVAGR
LHVEVMRVTG AVPERMAEDD SSENSSESGS LEVVDSSGEI IHRVKKLTCR VKIKEATGLP
LNLSNFVFCQ YTFWDQCEPT VAAPVVDPEV PSPQSKDAQY TVTFSHCQDY VVNVTEEFLE
FISDGALAIE VWGHRCTGNG SSIWEVDSLH AKTRTLHDRW NEVTRRIEMW ISILELNELG
EYAAVELHQA KDVNTGGVLQ LRQGHSRRVQ VTVKPVQHSG TLPLMVEAIL SISIGCITAR
STKLQRGLDS YQRDDEDGDD MDSYQEEDLN CVRERWSDAL IKRREYLDEQ IKKVSNKKEK
TEDDVEREAR LVEQWVGLTE ERNAVLVPAP GSGIPGAPAD WIPPPGMETH IPVLFLDLNA
DDLSANEQLV GPHASGVNSI LPKEHGSQFF YLPIIKHSDE EVSATASWDS SVHDSVHLNR
VTPQNERIYL IVKTTVQLSH PAAMELVLRK RIAANIYNKQ SFTQSLKRRI SLKNIFYSCG
VTYEIVSNIP KATEEIEDRE TLALMAARSE NEGTSDGETY IEKYTRGVLQ VENILSLERL
RQASNCRAVT VKEALSTKAR HLRRSLSTPN VHNVSSSRPD LSGFDDDDKG WPENQLDMSD
YSPSYQDVSC YGTLPRDSPR RSKEGCTSEN PHALTVSPFK AFSPQPPKFF KPLMPVKEEH
KKRIALEARP LLSQESMSPS QAHNPGCIVP SGSNGSSMPV ELNSKREKKI DSEEEENDLE
GLSRKLISSQ PYVPVEFADF SVYNASLENR EWFSSKGDLT NSKVLEKEVS RSPTTSSITS
GYFSHSASNA TLSDMVVPSS DSSDQLALPT KDTDSSEHPG PSLGQDFRPS SNKELTELER
GLGKDKMTVV PLKENSALAK GSPLSPSIPE KNSRTLCRTS SCSEQDACSS KNGQPAREFC
PREVTVEHTT NILEDHSFTE FMGVSDGKDF DGLTDSSAGE LSSRRNLPNT ADSRSFSHGP
QDPGQLCSSA ENDQVINSRG VSDRVDEPSW TMLTCCP
//
