ID A0A3B4U072_SERDU Unreviewed; 1753 AA.
AC A0A3B4U072;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Kinesin-like protein KIF13B {ECO:0000313|Ensembl:ENSSDUP00000011959.1};
GN Name=KIF13B {ECO:0000313|Ensembl:ENSSDUP00000011959.1};
OS Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000011959.1, ECO:0000313|Proteomes:UP000261420};
RN [1] {ECO:0000313|Ensembl:ENSSDUP00000011959.1}
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}.
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DR Ensembl; ENSSDUT00000012177.1; ENSSDUP00000011959.1; ENSSDUG00000008546.1.
DR GeneTree; ENSGT00940000155500; -.
DR OMA; KTRWESQ; -.
DR Proteomes; UP000261420; Unplaced.
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 GO; GO:0048731; P:system development; IEA:UniProt.
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; 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; 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}.
FT DOMAIN 10..348
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT DOMAIN 1667..1709
FT /note="CAP-Gly"
FT /evidence="ECO:0000259|PROSITE:PS50245"
FT REGION 543..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1371..1396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1415..1447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1467..1491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1555..1578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 363..405
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 606..638
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 556..574
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1377..1396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1425..1446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1476..1490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 105..112
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1753 AA; 196649 MW; 0AF5E42DE44F0BFF CRC64;
MGEPSLDDSN VKVAVRVRPM NRREKELNTK CVVEMVKNQT ILHPAGANLG KADTRYVFAY
DYCFWSMDET DKEKFAGQEV VFQCLGESLL YNAFQGYNAC IFAYGQTGSG KSYTMMGSGD
QPGLIPRLCS ALFERTQKEQ REEESFTVEV SYMEIYNEKV RDLLDPKGQT LRVREHKVLG
PYVDGLSRLA VASYKDIESL MSEGNKSRTV AATNMNEESS RSHAVFNIIL THTLKDLQSG
TSGEKVSRLS LVDLAGSERA AKTGAAGERL KEGSNINKYE NHSLMHLYFV IRDCPCFYNF
SLLLSSFRLQ DCLGGNSRTA MVATVSPSAD NYEETLSTLR YADRAKNIVN HAVVNEDPNA
RIIRELREEV EKLRVQLTQA ESLKAPELKE RLEESEKLIQ EMTITWEEKL RKTEEIAQER
QKQLESLGIS LQSSGIKVGD DKSFLVNLNA DPALNELLVY YLKEHTKVGS ADSQDIQLCG
MGIQAEHCVI DISAETAVIL TPYRNARTCV NGSPVTSALQ LHHGDRIFWG NNHFFRINLP
KRRSRGAEDE EGEGGVMKNS SSSEQLDADG DTASEVSSEV SFSYEFAQTE VMMKALGNND
PMQAVLQSLE RQHEEEKRSA LERQRQMYEQ ELQQLRKKLN PDRLSTGQQS HYRSLERLSI
GGMSHSSSAQ SRLRQWSEDR EVVLVRSLRR LREQIVRANL LVQEACFIAE ELERHTEYRV
TLQIPSDNLN ANRKRDAVLS EPAIQVRRRC RGKQIWSLEK MENRLVDMRE LYQEWQDYHL
HHHDNPVMRS YFRRADPFFD EQENHSLIGV ANVFLSCLFY DVKLQYAIPI INQKGEVAGR
LHVEVVRVGG GLEDNMAGGD EPDNNQDGEI QDRKLVCMIK ILQATGLPQY LSNFVFCQYS
FWDQPEPIIV APEVDPSSSS PSTKDPHCMV VFDSCKELAV SVTEDFIEYL TEGAVAIEVY
GHRQADAGRN PALWDLSIIQ AKTRTLRDRW SEVMRRLELW IQILEINENG DFVPVEVVPA
RDVRTGGIFQ LRQGQSRRIQ VDVRSVQDSG TMPLISEIVL AVSVGCVEIR NTTANQEIDE
MDSYQERDLE RLRRQWLAAL TKRQEYLDQH LQSLVSKAEK TEDDMEREAQ LLEWRLTLTE
ERNAVMVPSA GSGIPGAPAE WVPLPGMETH IPVLFLNLKP DDLSSQDQFE VPEAGGWDAT
LSGEDEDDFF DLQIVKHYDG EVKAEASWDS TVHECPQLSR GGAWPEQRVY LTVRVVVQLS
HPADMQLVLR KRICVNVNPG RQGFAHNFLR RMSTRSTIPG CGVTFEVVSN IPGDAPGSED
REMLARLAAS AHNSQSADDE AAIEKYLRSV LSLENILTLD RLRQEVAVKE QLAGRGRSNR
RSLSSPSVHR LSGSRQDLST TCLLDDKGRW ESQQDIFMPS HRTLPRPASS PSTYSTSPSS
SPTPFALVPQ MPKLLKSLFP VRDDKKELRP SPHNQQHVPR IMTSSGGDDN RLKTETVRLC
PVLFPEVPPL PVHDPHDTTP LSPLSQSSSG YFSTSVSTVT LSDVLQPSSS SSSLLAAETT
LPTNPQQQGA DRNDVVTSPS QCGAKMAVVA PQSSNSSANH NNVTAENSFS KQRLVNSGGG
GGEGFEQLEI FVDDEEHSHD DNLPDWLTEG AYVTVGGNKA GTVRYVGVTQ FAEGVWVGVE
LDTPVGKNDG SVGGHRYFHC KPGYGVLVRP DRLSSRDQTS RRTGEFAPSA HVPVLRREAI
VSRSRESRKS WSS
//
