ID A0A1V4JYD7_PATFA Unreviewed; 1951 AA.
AC A0A1V4JYD7;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Kinesin-like protein KIF13A isoform A {ECO:0000313|EMBL:OPJ76667.1};
GN Name=KIF13A {ECO:0000313|EMBL:OPJ76667.1};
GN ORFNames=AV530_016311 {ECO:0000313|EMBL:OPJ76667.1};
OS Patagioenas fasciata monilis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Patagioenas.
OX NCBI_TaxID=372326 {ECO:0000313|EMBL:OPJ76667.1, ECO:0000313|Proteomes:UP000190648};
RN [1] {ECO:0000313|EMBL:OPJ76667.1, ECO:0000313|Proteomes:UP000190648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BTP2013 {ECO:0000313|EMBL:OPJ76667.1};
RC TISSUE=Blood {ECO:0000313|EMBL:OPJ76667.1};
RA Soares A.E., Novak B.J., Rice E.S., O'Connell B., Chang D., Weber S.,
RA Shapiro B.;
RT "Band-tailed pigeon sequencing and assembly.";
RL Submitted (FEB-2016) 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 -!- 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:OPJ76667.1}.
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DR EMBL; LSYS01005643; OPJ76667.1; -; Genomic_DNA.
DR STRING; 372326.A0A1V4JYD7; -.
DR Proteomes; UP000190648; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
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; 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; 2.30.30.190; CAP Gly-rich-like domain; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR InterPro; IPR036859; CAP-Gly_dom_sf.
DR InterPro; IPR000938; CAP-Gly_domain.
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:SF5; -; 1.
DR PANTHER; PTHR47117; STAR-RELATED LIPID TRANSFER PROTEIN 9; 1.
DR Pfam; PF01302; CAP_GLY; 1.
DR Pfam; PF12473; DUF3694; 2.
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; SM01052; CAP_GLY; 1.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF74924; Cap-Gly domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS00845; CAP_GLY_1; 1.
DR PROSITE; PS50245; CAP_GLY_2; 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}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000190648}.
FT DOMAIN 1..354
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT DOMAIN 1878..1920
FT /note="CAP-Gly"
FT /evidence="ECO:0000259|PROSITE:PS50245"
FT REGION 1110..1129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1471..1490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1519..1544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1642..1680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1697..1719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 366..411
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 650..715
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1519..1536
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1644..1660
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1661..1680
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1700..1719
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 104..111
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1951 AA; 218492 MW; 5C83E4A40AD73512 CRC64;
MNTSLSQFSL ARLLSNQAAL GFMLDMVLIT CLKHDEHMHR SNSTCALLLW RSEDKVFAFD
HCFWSMDESN TTKYAGQEMV FKCLGEGILE KAFQGYNACI FAYGQTGSGK SFSMMGNAEQ
QGLIPRLCCA LFQRISVEEN ESHTFKVEVS YMEIYNEKVR DLLDPKGSRQ SLKVREHKVL
GPYVDGLSQL AVTNFEDIES LMSEGNKSRT VAATNMNEES SRSHAVFNII VTQTLYDLHS
GNSGEKVSKV SLVDLAGSER VSKTGAAGER LKEGSNINKS LSTLGLVISS LADQAAGKGK
NKFVPYRDSV LTWLLKDNLG GNSQTAMIAT ISPAADNYEE TLSTLRYADR AKRIVNHAVV
NEDPNARVIR ELREEVEKLK EQLSQAEAMK APELKEKLEE SEKLIKELTV TWEEKLRKTE
EIAQERQRQL ESMGISLESS GIKVGDDKCY LVNLNADPAL NELLVYYLKD HTRVGADTSQ
DIQLFGIGIQ PEHCEIDIAF DGEVTLTPKE NARSCVNGAL VCSVTQLWHG DRILWGNNHF
FRINLPKRKR RDWLKDLEKE TSLGEHDLDA TSEASSEPDY NYEFAQMEVI MKTLNSNGDE
FQMNLPSWWS SVLSSLLKSL LPVLRPQTIP YLCQNWDKDP VQNVVQILEK QYLEEKRSAL
EEQRLMYERE LELLRQQLSP ERQHQHSSDR LSYTAQTAQQ KVNLWTEERD ELFRQSLAKL
REQIVKANTL VREANFLAEE MSKLTDYQVT LQIPAENLSA NKKRGAIVSE PAIQVRRKGK
GTQVWTIEKL ENKLIDMRDL YQEWKEKVPE IRKLIGKRGD PFYEAQENHN LIGVANVFLE
CLFYDVKLQY AVPIISQQGE VAGRLHVEVM RVTGSVPERV VEGDDSSENS SESGSLEVMD
NNGEIIHRAK KLSCRVKIKE ATGLPLNLSN FVFCQYTFWD QCESVAAPVV DPDVPSPQSK
DAHFTVTFSH CKDYVVNVTE EFLEFISEGA LAIEVWGHRC TGNGSSVWEV DSLHAKTRTL
RDRWNEVTRR IEMWISIQEL NEMGEYTAVE LHQAKDVNTG GIFQLRQGHS RRVQVTVKPV
QHSGTLPLMV EAILSVSIGG VTARSTKLQR GLDSYQKEED DGGDMDSYQE EDLNCVRERW
SDALIKRREY LDEQIQKISN KQEKSEDDLE REARLVEQWV GLTEERNAVF VPAPGSGIPG
APADWIPPAG METHIPVLFL DLNADDLSAN EQLIGPHASG VNSILPKEHG SPFFYLPIIK
HSDDEVSATA AWDSSVHDSV HLNRVTPQNE RIYLIVKAIV QLSHPAAMEL VLRKRIAANI
YNKQSFTQSL KRRISLKNIY YACGVTYEIV SNIPKATEEI EDRETLALMA ARSENEGTSD
GETYIEKYTR GVLQVENILS LERLRQAVTV KEALSTKARN IRRSISTPNV HNVSCSRLDL
SACDEDDKGW AESHLDISDC SSSYQDVSCY GTLPRESPRK SKDGSGVVSE NSHALMASPF
KAFSPQPPKF FKPLMPVKEE HKRKTPLESR PLLSQEDSEE EDSELEAINK KLISPQSFQN
FRPYVPEEFA DFSVYNASLE NREWFSPKSD FMSSRVLEKE VSRSPTTSSI TSGYFSHSAS
NATLSDMLVP CSDSTDQLAT HTKELDSNDP SGSSLAHDLR SSSNKECREP EKELAREKLP
VLPLKENSAL AERVPLSLDA TDRDSQQLPR AGSFPALSSS AGKSTCRTIE FSAREATVEH
TTDILEDHSF TEFMGVEDGK DFDHLTAPQS CSLLSSNGAD ASELPRGAGV EQSMCVVQLG
SGDAVGNPLC LTLMKETSDP ETGPDAAIDY VIGKDHLDAS DCEEGASADQ ADVLPSWVAV
GEQVCVGSNK MGTVRYVGMV DFSAGIWVGV ELNVQLGKHN GTVKGREYFH CKPRHGIFLI
LGVALGVRQQ NLKASRNVFP RDADESLPIY C
//
