ID A0A3L8RBL8_CHLGU Unreviewed; 668 AA.
AC A0A3L8RBL8;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN ORFNames=DV515_00016952 {ECO:0000313|EMBL:RLV76462.1};
OS Chloebia gouldiae (Gouldian finch) (Erythrura gouldiae).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Passeridae;
OC Chloebia.
OX NCBI_TaxID=44316 {ECO:0000313|EMBL:RLV76462.1, ECO:0000313|Proteomes:UP000276834};
RN [1] {ECO:0000313|EMBL:RLV76462.1, ECO:0000313|Proteomes:UP000276834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red01 {ECO:0000313|EMBL:RLV76462.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:RLV76462.1};
RX PubMed=30282656;
RA Toomey M.B., Marques C.I., Andrade P., Araujo P.M., Sabatino S.,
RA Gazda M.A., Afonso S., Lopes R.J., Corbo J.C., Carneiro M.;
RT "A non-coding region near Follistatin controls head colour polymorphism in
RT the Gouldian finch.";
RL Proc. R. Soc. B 285:0-0(2018).
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283,
CC ECO:0000256|RuleBase:RU000394}.
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:RLV76462.1}.
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DR EMBL; QUSF01000614; RLV76462.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L8RBL8; -.
DR Proteomes; UP000276834; Unassembled WGS sequence.
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; cd01369; KISc_KHC_KIF5; 1.
DR Gene3D; 6.10.250.1590; -; 1.
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:SF56; KINESIN MOTOR DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00225; Kinesin; 2.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Microtubule {ECO:0000256|RuleBase:RU000394};
KW Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283,
KW ECO:0000256|RuleBase:RU000394};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00283}; Reference proteome {ECO:0000313|Proteomes:UP000276834}.
FT DOMAIN 9..401
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 444..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 487..588
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 86..93
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 668 AA; 74061 MW; 154544D67C2B6EF5 CRC64;
MAEPSSECSI KVLCRFRPLN QAEILRGDKF LPVFQGDDSV VVGGKPYVFD RVFPPNTTQE
QVYHACAMQI VKDVLAGYNG TIFAYGQTSS GKTHTMEGKL HDPQQMGIIP RIARDIFNHI
YSMDENLEFH IKVSYFEIYL DKIRDLLDSE WGGTGGYWWA LGSTGSHWED LEANSGGLGS
YWKDWEVTGE HWVVTGEHWV VSGGHWVVSG GHWELLERCG RPQPLLSPSV TKTNLAVHED
KNRVPYVKPF WGAAGALPVL GCPQRVPLPA DMNEHSSRSH SIFLIHIKQE NVETEQKLSG
KLYLVDLAGS EKVSKTGAEG AVLDEAKNIN KSLSALGNVI SALAEGTKAY VPYRDSKMTR
ILQDSLGGNC RTTMFICCSP SSYNDAETKS TLMFGQRAKT IKNTASVNLE LTAEQWKKKF
EKEKEKNKAL RETLARLEAE LSRWRSGEAV PETEQLNEAE AGTGPGEGQG GAPEEPPMND
NSSSIVIHIS DEERHKYEEE IRKLYKQLDD KDDEINQQSQ IMEKLKQQML DQEEVLAVAR
GGGEAARREL AALRAEHGAA RAEVTEVLAA LEELARSYDR KAQEAEDTGR HNRRLADELA
RTEATTLSLE SELSRARELG GQQRRRAAEV LNGLLRDLSE LSALVGSGDI KLVRGTGHRE
HGAGGSVP
//
