ID   A0A3B4WB47_SERLL        Unreviewed;      1406 AA.
AC   A0A3B4WB47;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Kinesin-like protein KIF16B {ECO:0000313|Ensembl:ENSSLDP00000001379.1};
GN   Name=KIF16B {ECO:0000313|Ensembl:ENSSLDP00000001379.1};
OS   Seriola lalandi dorsalis.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangiformes; Carangidae; Seriola.
OX   NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000001379.1, ECO:0000313|Proteomes:UP000261360};
RN   [1] {ECO:0000313|Ensembl:ENSSLDP00000001379.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00283}.
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DR   Ensembl; ENSSLDT00000001460.1; ENSSLDP00000001379.1; ENSSLDG00000001098.1.
DR   GeneTree; ENSGT00940000162838; -.
DR   Proteomes; UP000261360; Unplaced.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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   GO; GO:0048731; P:system development; IEA:UniProt.
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:SF6; KINESIN-LIKE PROTEIN KIF1C ISOFORM X1; 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};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          1..257
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          587..632
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          646..667
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          716..735
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          906..1014
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1372..1398
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          746..773
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        587..614
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        906..1002
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1406 AA;  160090 MW;  FF7100B337C8B887 CRC64;
     MTLCSVSETG FSSFQGDAGL IPRICEGLFS RISDATRWDV ASFRTEVSYL EIYNERVRDL
     LRRKSTQTYN LRVREHPKDG PYVEDLSKHL VQNYSDVEEL MEAGNINRTT ASTGMNDVSS
     RSHAIFTINF TQAKFDAEMP SETVSKIHLV DLAGSERADA TGATGVRLKE GGNINKSLVT
     LGNVISALAD MTQDGVNTNL KKKSVFVPYR DSVLTWLLKD SLGGNAKTIM IATVSPADVN
     YGETLSTLRY ANRAKNIINK PTINEDANVR LIRELRAEIA RLKALLIQGN QIALLDSPTA
     LSMEEKLHQN EARVLELTKE WTNKWNETQN ILKEETLALR KEGIGVVLDS ELPHLIGIDD
     DLLSTGIILY HLKEGRTYVG REDASTEQDI ILHGLDLESE HCKFENQNGT VTLVPLGGAQ
     CSVNGVQVTE PSQLNQGAVI LLGRTNMFRF NHPKEAAKLR EKRKSGLLST FSLSMTDLSK
     SCENLSTVML YNPGLFTEKG PVFLRLEFER QQREELEKLE LKRRLINDME AKQQSEKVEL
     ERLQQEVESQ RKESEEVQQR ILRQEESLRR RSQDIESRLR DFLAEKERFE EERRSEPPGE
     ELQRRQRQNQ QQEGEAEEEQ DEEQRLQQEA AEQTEIYREL ERLKREREEQ KVRLEAERRR
     LEEQEREQLS LVGRLEEQLR EKHEAATTLL TREDARRLEE ERRALAEIRG ELLRAKETGE
     RPDVEDSGEE ARSAQARYTD FKAAQVKELG QLEEGLRQQR ERLEKEVTAE RSTVLLLAHG
     LRERQQQLKE TQEKGAQDAT AVCQEEQLVK QAEHRLQFKE RQLVSLADGL LPALAEEKQR
     AVEMLERSSG GSNGNCDSPP GLDNTLFQVE KELEDKEDKL NLHWHSAQQL QQLQETYEFT
     ANVARQEEKV RRKEKEILES KEKQQREAME QAVARLERRH SALRRSVSLE PDTEEQRHKS
     SVQRNLRGTD LDQQRVEQEI QKLRQRISEG EENNRTHSVS NEEKTSHGSS PVSHIQSLNT
     LLPLSDDRIN AYIEEEVQRR LRKMNLLNGG SSMDLSLSCE SLREEEEVSD CSSVRLTDED
     DEKLKNINPR RHKYERACRL WSRSLSATEL EANSPPKVEQ NALEEAENVI LKLPREETLV
     STAEVLIGKE VPYKDGGKNT GWHAGVNIPL RDELFCVNSA KTKSNRFDEN ENIADKRRTD
     SAGCVLDDEK VEDRPKELLV NGRSNVKHQT CDPGAVEDAE LPSDQLSQDS VNGCVTSKQK
     SKECVNGQTK RETDAEAEKV ATNASYVLGY FTGKLSEAYK DAGRRLQGTR DIIRNVGTGE
     MKVVLSQYVT MMSNELPLIH RTQLKPQPEP CMRAANKVSL VDLSRDRALS LHQNTGESVT
     PGVSGRPEGS VSSFKNTGPQ VFYQRL
//