ID A0A0Q3MUC9_AMAAE Unreviewed; 1901 AA.
AC A0A0Q3MUC9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Kinesin-like protein KIF13B {ECO:0000313|EMBL:KQK85967.1};
GN ORFNames=AAES_37791 {ECO:0000313|EMBL:KQK85967.1};
OS Amazona aestiva (Blue-fronted Amazon parrot).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Amazona.
OX NCBI_TaxID=12930 {ECO:0000313|EMBL:KQK85967.1, ECO:0000313|Proteomes:UP000051836};
RN [1] {ECO:0000313|EMBL:KQK85967.1, ECO:0000313|Proteomes:UP000051836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FVVF132 {ECO:0000313|EMBL:KQK85967.1};
RA Gilbert D.G.;
RL Submitted (OCT-2015) 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:KQK85967.1}.
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DR EMBL; LMAW01000703; KQK85967.1; -; Genomic_DNA.
DR STRING; 12930.A0A0Q3MUC9; -.
DR Proteomes; UP000051836; 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; 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; 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; 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}; Coiled coil {ECO:0000256|ARBA:ARBA00023054};
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:UP000051836}.
FT DOMAIN 1..335
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT DOMAIN 1786..1828
FT /note="CAP-Gly"
FT /evidence="ECO:0000259|PROSITE:PS50245"
FT REGION 494..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1335..1403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1425..1691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1716..1752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1873..1901
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1335..1398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1436..1484
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1492..1535
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1569..1602
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1609..1657
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1716..1741
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 85..92
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1901 AA; 212328 MW; B98C4D3DAEC90C97 CRC64;
MCKFIMWTKD EFRKFRDTEE YCETLETLDF TFFHSTVFAY DHCFWSMDES VKEKYAGQDV
VFKCLGENIL QNAFEGYNAC IFAYGQTGSG KSYTMMGTAD QPGLIPRLCS GLFERAQKEE
NEEQSFKVEV SYMEIYNEKV RDLLDPKGSR QSLKVREHSV YGPYVDGLSK LAVASYKDIE
SLMSEGNKSR TVAATNMNEE SSRSHAVFKI ILTHTLYDVQ SGTSGEKVGK LSLVDLAGSE
RATKTGAAGD RLKEGSNINK SLTTLGLVIS ALADQAAGKN KNKFVPYRDS VLTWLLKDSL
GGNSKTAMVA TVSPAADNYD ETLSTLRYAD RAKNIVNHAV VNEDPNARII RELREEVEKL
REQLTKAEAM KSPELKERLE ESEKLIQEMT VTWEEKLRKT EEIAQERQKQ LESLGISLQS
SGIKVGDNKC FLVNLNADPA LNELLVYYLK EHTLIGSDNS QDIQLCGMGI LPEHCIIDIT
PEGQVMLTPK KNTRLNLPKK KKKADHEDEE RDNSMKCSNS VEQLDIDGDN SSEVSSEINF
SYEYAQMEVT MKALGSNDPM QSILQSLEQQ HQEEKRSALE RQRLMYEHEL EQLRRRLSPE
KQHFRSMDRF SFHSPSAQQR LRQWAEEREE MLTHSLRRLR EQIVKANXYV REANFIGEEL
DKRTEYKVTL QIPASSLNAN SKRGAILSEP AIQVRRKGKG KQIWSLEKLE NRLVDMRDLY
QEWKDCEEDN PVMRAYFRRA DPFYDEQENH SLIGVANVFL ECLFYDVKLQ YAVPIINQKG
EVSGRLHXEV VRVSGEIDDR LVGGEDSPDY SNENDVQERK LVCRIKILQA TGLPQHLSNF
VFCKYTFWDQ LKPVDVAPEV DPSLSSVSKE PRCMVVFDHC NEVSVNISED FMEHLYDGAL
AIEVYGHKQS GDRKNPALWD LGIIQAKTRS LRDRWSEVTR KVELWVRILE LNENGEYCPV
EVTPARDVCT GGIFQLRQGQ SRRIQVEVRS VQESGTLPLM EESILSVGIG CVQIKHVKSQ
KLPENYQEEE DEMDSYQDRD LERLRRKWLC ALTKRQEYLD QQLQKLVGKP DKTEDDADRE
AQLLEMRLTL TEERNAVMVP SAGSGIPGAP AEWTPVPGME THIPVIFLDL NADDFSSQDN
LDDPEAGGWD ATLVAEEEEE FFELQIVKHH DSEVKAEASW DSTVHDCIQL SKGTAADERV
YLIVRATVQL SHPAEMQLVL RKRICVNVYG RQGFAQSFLR RMSHRSSIPG CGVTFEIVSN
IPEDAQGAEE REALARMAAN VEDAASADSE AYIEKYLRSV LAVENILTLD RLRQEVAVKE
QLMGKGKLYR RSLSSPSVNR LSGSRQDLAP PYNLSSNRGR WESQQDVSQG ATNSSRGISP
SRTSLPGSRQ QNHSPDPGIG SLAASYLNPV KSFVPQMPKL LKSLFPVRDD KKGRQTSPLA
QQAVPRIMVQ SASXDTSAAR MKQINQEEIG KQLFETAVQT SEVDKSPEKT PKVPLQQPSG
DTQAQESQEG PPSPLSEASS GYFSHSVSTA TLSEALAAGS DAVAQPGSQA PAASDFPXPA
VAHVPSSDMP EHSDSSSESC LSTKRENLPA FSLQSTHARP KDSTEVNGND ALKSKSCISP
VTQSEQGNDA SVATDAKTFL STSTPKKELL SKQLMESTGQ VRKKEMASGS SELGFPKPQI
HPEQLSQPGV AASPFKIQKV KTSELKSFTS MLGTDPMYSL NTEEQQEGEK STSTAHGLNH
NGSETAEEKL EVASDSEDAN EIPEWLKEGE YVTVGANKTG TVRYIGPTDF QEGTWVGVEL
DLPSGKNDGS IGGKQYFRCN PGYGLLVKPG RVKKATGSAR RRSTGLRLQG GVATENRRSG
SFSSSASNLA SLTALAKSEG GPTLRLEKSQ KNAENRKSWA N
//
